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Observations on the Orientation of Keratin in Thickened Cornified Epithelium of the Human Skin1
OBSERVATIONS ON THE ORIENTATION OF KERATIN IN THICKENED CORNIFIED EPITHELIUM OF THE HUMAN SKIN* A. (lEDION OEDEONMATOLTSY, MATOLTSY,M.D. MI). AN!) AN!)GEORGE GEORGEF. F.ODLAND, ODLAND,M.D. MI).
It has been amply demonstrated that mammalian keratins are built up of parallel-oriented chain molecules which show a characteristic characteristic x-ray x-ray diffraction diffraction spectrum and reveal positive double refraction with respect to the long axis of chain molecules (1—6). In Iii the cortex of the hair, keratin was found oriented parallel to the longitudinal axis of the hair, while in the nail the orientation was
perpendicular to the longitudinal axis of the nail plate (1, (1, 2, 2, 3). 3). In In the the only only stratified squamous epithelium heretofore regarded as suitable for x-ray study, i.e., snout of the cow and horse horse burr, burr, the the chain cham molecules inoleules of ofkeratin keratin were were found found to be oriented parallel to the surface of the skin. Detailed information has not yet been obtained on the orientation of keratin in thickened cornified epithelium of human skin, such as the callus. The callus, in contrast to the hair or nail, is a very complex tissue, since it contains various
structural differentiations, such as the surface grooves and ridges. It is also perforated by numerous sweat ducts. The individual cells cells are are laid laid down down in in apparent relationship to these gross structures, hence differently oriented components might be expected in various regions of this keratinous tissue. In the present study, the structure of callus was investigated by the polarization optical method (7). The interference colors, produced by various regions of the callus, were studied and from the results, conclusions were drawn about the direction direction of of keratin keratinorientationi. orientation. MATERIAL ANI) METHOD
For the present study, small pieces of human callus taken from the sole of the foot were selected. All pieces showed regular, parallel, straight grooves and ridges on the surface. These pieces of callus were softened in distilled water for 24 to 48 hours at into pieces pieces 3—4 3—4mm. mm.square squareand and1—2 1—2mm. mm.thick. thick.They They 5°C. and subsequently cut into were mounted on blocks by freezing, so that the surface surface plane plane of of callus callus was was kept kept parallel to the upper surface of the block. In order to obtain obtain well well oriented, oriented, horhorizontal sections from the callus, great care was used in mounting and sectioning the specimens. specimens. Horizontal, Horizontal, serial serialsections sections2O—3O 20—30 thick thiek were cut at —20°C. —20°C. in in the Linderstrom-Lang Linderstrom-Lang freezing freezing cabinet. cabinet.The Thesections sectionswere weredried driedOfl on slides slides at at room temperature without being mounted or covered. * From the Dermatological Research Laboratories of the Department of Dermatology, Harvard Medical School, at the Massachusetts General Hospital, Boston 14, Massachusetts. a.sachuetts.
This investigation was supported by aa research research grant grant RG-3921 RG-3921 (c) (c) from from the the NaNampported by
tional Institutes of Health, Public Publio Health Service. Presented at the Sixteenth Annual Meeting of The Society for Investigative 1)ermaDermatology, Inc., Atlantic City, N. J., June 4, 1955. 121
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THE JOURNAL OF INVESTIGATIVE DERMATOLOGY
For the polarization optical studies, a Leitz research type of polarizing microscope was used. The interference colors were studied by using a first-order red retardation plate. This was inserted into the microscope so that its slow axis ('ye) formed an angle of —45° with the polarizer axis (Fig. 1A). Under such conditions, the field of the microscope showed a uniform red color. If the retar-
dation of a structure was added to the retardation of the plate and an interference color such as blue was seen, the sign of double refraction was considered positive and the molecular chains of keratin were considered to lie parallel to
the slow axis of the plate (Fig. IB). If a component structure showed a subtraction color, such as yellow, the chain molecules were regarded as lying with their long axes perpendicular to the slow axis of the plate (Fig. 1C) (For details of physical optics see reference 7). In either instance, double refraction was referred to some characteristic structural feature of the callus. RESULTS
Examination of serial sections under low magnification of the polarizing microscope clearly demonstrated that optically the callus is composed of two different types of regularly alternating, elongated areas. One of these areas P0 Pa
AN
BLUE
COLOP ADDITION COLOR
YELLOW SUBTRACTiON COLOR
FIG. 1. Method of using first-order red plate in the polarizing microscope to determine the direction of orientation of keratin chain molecules on the basis of interference colors. A: demonstrates the position of slow axis (yc) (ye) of the plate with respect to the axis of the
polarizer (P0) pnlarizer (PU)and andthe theaxis axisof ofthe theanalyzer analyzer(AN). (AN).BBand andC: C:demonstrate demonstrateaddition additionand and subtraction colors respectively respectively caused caused by by chain chain molecules molecules being being oriented oriented parallel parallel(B) (B)or or perpendicular perpendicular (C) to the slow axis (ye) of the plate.
123
ORIENTATION OF KE1IATIN KE1IATIN IN IN COENIFIE!) COISNIFIEPEPITI-TELIUM EPITHEIJIUM
PT a,-.
B
A
FIG. 2. A: horizontal section of human callus in polarized light. Narrow bright lines lilies eurrespond to grooves; wide and dark areas to ridges. B: the same section in ordinary correspond light.
—AN
P FIG. 3. Horizontal section of human callus in polarized light. Parallel birefringent hirefringent lines correspond to groove areas; the birefringent crossbauds crossbands are ale component structures of ridge analyzer axis. axis. areas. P0: polarizer axis; AN: AN analyzer
occurred beneath the surface grooves (sulci cutis) eutis) (Fig. 2A), the other beneath the surface ridges (cristae (cristac cutis). In ordiuary ordinary light these different parts of the callus were almost indistinguishable (Fig. 2B), but in ill polarized light they could easily he seen (Fig. 2A). By using the first-order red plate plate in in the the polarizing polarizing microscope, the following observations were made:
124
THE J0U1NAL Tfl1 JOURNALOF OFINVESTIGATIVE INVESTIGATIVEDEEMATOLOGY DERMATOLOGY
AN—
—AN
PD P0 FIG. 4. Horizontal section of human callus in polarized light showing circumferentially oriented oriented cornified cornified cells cells around around the the sweat sweat ducts. ducts. PU: PU: polarizer polarizer axis; axis; AN: AN: analyzer analyzer axis. axis.
Groove areas.—Each groove area showed maximal brightness if its longitudinal
axis was wasset settoto—45° 450 from from the polarizer axis (Fig. 3), indicating linear and axial orientation of keratin in these areas of the callus. callus. When When the the retardation retardation plate was inserted into the microscope and the longitudinal axis of groove areas was set to —45° (position shown in Fig. 3), each groove area showed a blue interference color, revealing positive sign of double refraction with reference to the longitudinal axis (compare with Fig. 1B). Consequently, it was concluded that in groove areas the long axis of chain molecules of keratin is preferentially oriented parallel to the longitudinal axis of grooves. Ridge areas.—In most sections, midway between neighboring sweat ducts, intensely birefringent cross-bands were seen connecting adjacent groove areas in a more or less transverse direction (Fig. 3). When the the retardation retardation plate plate was was inserted into the polarizing microscope, the cross-bands in the position shown
in Fig. 3 (oriented with the long axis at + 45°) showed a yellow subtraction color. This indicated that the preferential orientation of keratin chain molecules iii cross-band areas of the callus is transverse (compare Fig. 1C) and at right in angles to the chain molecules of groove areas. In a narrow region around the sweat ducts (Fig. 4), the single cornified cells showed positive index ellipsoids with long axes oriented circumferentially (Maltese cross) revealing an annularly oriented keratin structure. structure. Surrounding Surrounding the the sweat duct regions, a random orientation was seen roughly forming concentric rings.
ORIENTATION OF KERATIN KERATIN TN IN CORNIFIED CORNIFIED ET'ITHELIUM
125
DISCUSSION
Although x-ray analysis of hair, nail, and cormhed coriiihed epithelium of the skin shows that their structures are built up of similar aipha-keratin molecules (2, 3, 5), differences appear in the orientation of aipha-keratins alpha-keratins in the various horny tissues. Whereas in the hair and nail, orientation is linear, in thickened cornified epitheliurn a complex structure seems to prevail. The above observations indicate that the groove areas, together with cross-
band regions of ridge areas, form a lattice-like pattern in iii thickened cornified epitheliurn of the human skin. This lattice structure is schematically shown epithelium showii in iii Fig. 5. Functionally, the lattice structure may increase the mechanical strength of the cornified epithelium and assure isodimensional physical response to me-
Fi;. 5. Fie. 5. Schematic Schematic picture of oriented areas of human callus caIIu in in horizontal horizontal section. section.
chanical stress. The annular structure around the sweat ducts appears as an important support for the wall of the sweat duct and may assure its patency. SUMMARY
Polarization optical studies of serial sectioiis sections cut parallel to the surface of human callus showed that beneath the surface grooves, grooves, keratin keratin is is oriented oriented paralparallel to the surface plane and to the direction of the grooves. Beneath the ridges, a transverse orientation prevails, except in sweat duct regions which show an annularly oriented structure. The authors' sincere thanksarc aredue dueto toMrs. Mrs. Margit Margit Matolt.y Matoltsyfor forher hervaluable valuable assistance. assistance. ineere thanks
REFERENCES 1. Sciirsiiwr, ScHii1DT,W. W.J.: J.:Die DieBausteine Bausteinedes desTierkorpers Tierkörpersin inpolarisiertem polarisiertemLichte, Lichte,p. p.336. 336.Bonn, Bonn, Verlag von F. Cohen, 1924.
126
THE JOURNAL JOURNALOF OFINVESTIGATIVE INVESTIGATIVE DERMATOLOGY DERMATOLOGY
2. ASTBUEY, H. J.: J.: ASTBURY,W. W. T. T. AND AND Woons, Woons, H.
related fibers.
X-ray studies uf of the structure of hair, wool and
1934. A), 232: 333, A), 333, 1934. 3. J. C., HEEINGA,G. C.C. C.AND ANDWEIDINGER, WEIDINGER, A.: A.: On On keratin keratin and and cornification. cornification. 3.DEEK5EN, DIwcsiN, J. C.,HERINGA,
Phil. Tr. Roy. Soc. London, (Ser. (Ser.
Acta nccrl. neerl. Morphol., Morphol., 1: 1: 31, 31, 1937. DEEKsEN, C. AND ANDHERINGA, HERINGA,G. C.C.: C.:Verhornung Vcrhornungund undTonofibrillen Tonofibrillender derEpidermis. Epidermis. DERKSEN, J.J.C. Caz. lek., Gaz. lek., 15: 15: 532, 1936. 5. Cxuouo, A.AND AND CHAMPETIER, Recherches sur ics les roentgenogrammes roentgcnogrammes des kcratincs. CHAMPETIER, C.: Rccherches keratine. GIROUD,A. Bull. Soc. Soc. chim. chim. biol., 18: 656, 1936. 6. MATOLTsY, G.G.AND ANDODLAND, ODLAND,G.C.F.:F.:Tnvestigation Investigationof ofthe thestructure structure of of the the cornified cornificd MATOLTSY, A.A. epithelium cpithclium of of the the human human skin. skin. J. J. Biophysic. Biophysic. and and Biochem. Biochem. Cytol., Cytol., 1: 1: 191, 191, 1955. 1955. 7. BENNETT, H. S.: The microscopical investigation of biological materials with polarized 4. 4.
light. In TnMcClung's McClung'sHandbook Handbookof ofMicroscopical MicroscopicalTechnique Technique(H. (R.McClung McClungJones, Jones, Editor), p. 591. 591. New New York, York,Paul PaulB. B.Hoeber, Hoeber,Tnc., Inc., 1950. 1950.
DISCUSSION DR. FLESCH (Philadelphia, Penna.): I would DR. PETER PETER FLESCH (Philadelphia, Penna.): I would like like pointout outthat that totopoint such differences in keratin exist not only in calluses, but in normal epidermis. In an admirable work (Anat. Rec. 119: 449, 1954), it has been shown that different types of keratin occur on the skin of the finger tips and that these differences contribute to the tactile sensitivity. Da. VAN SCOTT Dn.EUGENE EUGENEJ. J. VAN SCOTT (Bethesda, Md.): I wouldlike liketotoask askDr. Dr.Matoltsy Matoltsy Md.): I would (Bethesda, what the anatomical relationship relatiollship of the sweat duct is to the dermal papilla. Dn. DR.A. A.GEDEON GEnEONMATOLTSY MATOLTSY closing): closing): WeWe have have studied studiedvery veryfew fewfull fullthickthick(in (in
ness skins by this method, so I don't think I can answer the question that Dr. Van Scott asks. asks. These These were were callus callussections sectionsand anddidn't didn'tcontain containany ay other part of the skin—only the cornified epithelium. epitheliurn.
THE JOURNAL OF INVESTIGATIVE DERMATOLOGY
94
linolenic acid extract. Arch. This pdf is a scanned copy UV of irradiated a printed document.
24. Wynn, C. H. and Iqbal, M.: Isolation of rat
skin lysosomes and a comparison with liver Path., 80: 91, 1965. and spleen lysosomes. Biochem. J., 98: lOP, 37. Nicolaides, N.: Lipids, membranes, and the 1966.
human epidermis, p. 511, The Epidermis
Eds., Montagna, W. and Lobitz, W. C. Acascopic localization of acid phosphatase in demic Press, New York. human epidermis. J. Invest. Derm., 46: 431, 38. Wills, E. D. and Wilkinson, A. E.: Release of 1966. enzymes from lysosomes by irradiation and 26. Rowden, C.: Ultrastructural studies of kerathe relation of lipid peroxide formation to tinized epithelia of the mouse. I. Combined enzyme release. Biochem. J., 99: 657, 1966. electron microscope and cytochemical study 39. Lane, N. I. and Novikoff, A. B.: Effects of of lysosomes in mouse epidermis and esoarginine deprivation, ultraviolet radiation and X-radiation on cultured KB cells. J. phageal epithelium. J. Invest. Derm., 49: 181, 25. Olson, R. L. and Nordquist, R. E.: Ultramicro-
No warranty is given about the accuracy of the copy.
Users should refer to the original published dermal cells. Nature, 216: 1031, 1967. version of1965. the material. vest. Derm., 45: 448, 28. Hall, J. H., Smith, J. G., Jr. and Burnett, S. 41. Daniels, F., Jr. and Johnson, B. E.: In prepa1967.
Cell Biol., 27: 603, 1965.
27. Prose, P. H., Sedlis, E. and Bigelow, M.: The 40. Fukuyama, K., Epstein, W. L. and Epstein, demonstration of lysosomes in the diseased J. H.: Effect of ultraviolet light on RNA skin of infants with infantile eczema. J. Inand protein synthesis in differentiated epi-
C.: The lysosome in contact dermatitis: A ration. histochemical study. J. Invest. Derm., 49: 42. Ito, M.: Histochemical investigations of Unna's oxygen and reduction areas by means of 590, 1967. 29. Pearse, A. C. E.: p. 882, Histochemistry Theoultraviolet irradiation, Studies on Melanin, retical and Applied, 2nd ed., Churchill, London, 1960.
30. Pearse, A. C. E.: p. 910, Histacheini.stry Thearetscal and Applied, 2nd ed., Churchill, London, 1960.
31. Daniels, F., Jr., Brophy, D. and Lobitz, W. C.: Histochemical responses of human skin fol-
lowing ultraviolet irradiation. J. Invest. Derm.,37: 351, 1961.
32. Bitensky, L.: The demonstration of lysosomes by the controlled temperature freezing section method. Quart. J. Micr. Sci., 103: 205, 1952.
33. Diengdoh, J. V.: The demonstration of lysosomes in mouse skin. Quart. J. Micr. Sci., 105: 73, 1964.
34. Jarret, A., Spearman, R. I. C. and Hardy, J. A.:
Tohoku, J. Exp. Med., 65: Supplement V, 10, 1957.
43. Bitcnsky, L.: Lysosomes in normal and pathological cells, pp. 362—375, Lysasames Eds., de Reuck, A. V. S. and Cameron, M. Churchill, London, 1953.
44. Janoff, A. and Zweifach, B. W.: Production of inflammatory changes in the microcirculation by cationic proteins extracted from lysosomes. J. Exp. Med., 120: 747, 1964.
45. Herion, J. C., Spitznagel, J. K., Walker, R. I. and Zeya, H. I.: Pyrogenicity of granulocyte lysosomes. Amer. J. Physiol., 211: 693, 1966.
46. Baden, H. P. and Pearlman, C.: The effect of ultraviolet light on protein and nucleic acid synthesis in the epidermis. J. Invest. Derm.,
Histochemistry of keratinization. Brit. J. 43: 71, 1964. Derm., 71: 277, 1959. 35. De Duve, C. and Wattiaux, R.: Functions of 47. Bullough, W. S. and Laurence, E. B.: Mitotic control by internal secretion: the role of lysosomes. Ann. Rev. Physiol., 28: 435, 1966. the chalone-adrenalin complex. Exp. Cell. 36. Waravdekar, V. S., Saclaw, L. D., Jones, W. A. and Kuhns, J. C.: Skin changes induced by
Res., 33: 176, 1964.
It has been amply demonstrated that mammalian keratins are built up of parallel-oriented chain molecules which show a characteristic characteristic x-ray x-ray diffraction diffraction spectrum and reveal positive double refraction with respect to the long axis of chain molecules (1—6). In Iii the cortex of the hair, keratin was found oriented parallel to the longitudinal axis of the hair, while in the nail the orientation was
perpendicular to the longitudinal axis of the nail plate (1, (1, 2, 2, 3). 3). In In the the only only stratified squamous epithelium heretofore regarded as suitable for x-ray study, i.e., snout of the cow and horse horse burr, burr, the the chain cham molecules inoleules of ofkeratin keratin were were found found to be oriented parallel to the surface of the skin. Detailed information has not yet been obtained on the orientation of keratin in thickened cornified epithelium of human skin, such as the callus. The callus, in contrast to the hair or nail, is a very complex tissue, since it contains various
structural differentiations, such as the surface grooves and ridges. It is also perforated by numerous sweat ducts. The individual cells cells are are laid laid down down in in apparent relationship to these gross structures, hence differently oriented components might be expected in various regions of this keratinous tissue. In the present study, the structure of callus was investigated by the polarization optical method (7). The interference colors, produced by various regions of the callus, were studied and from the results, conclusions were drawn about the direction direction of of keratin keratinorientationi. orientation. MATERIAL ANI) METHOD
For the present study, small pieces of human callus taken from the sole of the foot were selected. All pieces showed regular, parallel, straight grooves and ridges on the surface. These pieces of callus were softened in distilled water for 24 to 48 hours at into pieces pieces 3—4 3—4mm. mm.square squareand and1—2 1—2mm. mm.thick. thick.They They 5°C. and subsequently cut into were mounted on blocks by freezing, so that the surface surface plane plane of of callus callus was was kept kept parallel to the upper surface of the block. In order to obtain obtain well well oriented, oriented, horhorizontal sections from the callus, great care was used in mounting and sectioning the specimens. specimens. Horizontal, Horizontal, serial serialsections sections2O—3O 20—30 thick thiek were cut at —20°C. —20°C. in in the Linderstrom-Lang Linderstrom-Lang freezing freezing cabinet. cabinet.The Thesections sectionswere weredried driedOfl on slides slides at at room temperature without being mounted or covered. * From the Dermatological Research Laboratories of the Department of Dermatology, Harvard Medical School, at the Massachusetts General Hospital, Boston 14, Massachusetts. a.sachuetts.
This investigation was supported by aa research research grant grant RG-3921 RG-3921 (c) (c) from from the the NaNampported by
tional Institutes of Health, Public Publio Health Service. Presented at the Sixteenth Annual Meeting of The Society for Investigative 1)ermaDermatology, Inc., Atlantic City, N. J., June 4, 1955. 121
122
THE JOURNAL OF INVESTIGATIVE DERMATOLOGY
For the polarization optical studies, a Leitz research type of polarizing microscope was used. The interference colors were studied by using a first-order red retardation plate. This was inserted into the microscope so that its slow axis ('ye) formed an angle of —45° with the polarizer axis (Fig. 1A). Under such conditions, the field of the microscope showed a uniform red color. If the retar-
dation of a structure was added to the retardation of the plate and an interference color such as blue was seen, the sign of double refraction was considered positive and the molecular chains of keratin were considered to lie parallel to
the slow axis of the plate (Fig. IB). If a component structure showed a subtraction color, such as yellow, the chain molecules were regarded as lying with their long axes perpendicular to the slow axis of the plate (Fig. 1C) (For details of physical optics see reference 7). In either instance, double refraction was referred to some characteristic structural feature of the callus. RESULTS
Examination of serial sections under low magnification of the polarizing microscope clearly demonstrated that optically the callus is composed of two different types of regularly alternating, elongated areas. One of these areas P0 Pa
AN
BLUE
COLOP ADDITION COLOR
YELLOW SUBTRACTiON COLOR
FIG. 1. Method of using first-order red plate in the polarizing microscope to determine the direction of orientation of keratin chain molecules on the basis of interference colors. A: demonstrates the position of slow axis (yc) (ye) of the plate with respect to the axis of the
polarizer (P0) pnlarizer (PU)and andthe theaxis axisof ofthe theanalyzer analyzer(AN). (AN).BBand andC: C:demonstrate demonstrateaddition additionand and subtraction colors respectively respectively caused caused by by chain chain molecules molecules being being oriented oriented parallel parallel(B) (B)or or perpendicular perpendicular (C) to the slow axis (ye) of the plate.
123
ORIENTATION OF KE1IATIN KE1IATIN IN IN COENIFIE!) COISNIFIEPEPITI-TELIUM EPITHEIJIUM
PT a,-.
B
A
FIG. 2. A: horizontal section of human callus in polarized light. Narrow bright lines lilies eurrespond to grooves; wide and dark areas to ridges. B: the same section in ordinary correspond light.
—AN
P FIG. 3. Horizontal section of human callus in polarized light. Parallel birefringent hirefringent lines correspond to groove areas; the birefringent crossbauds crossbands are ale component structures of ridge analyzer axis. axis. areas. P0: polarizer axis; AN: AN analyzer
occurred beneath the surface grooves (sulci cutis) eutis) (Fig. 2A), the other beneath the surface ridges (cristae (cristac cutis). In ordiuary ordinary light these different parts of the callus were almost indistinguishable (Fig. 2B), but in ill polarized light they could easily he seen (Fig. 2A). By using the first-order red plate plate in in the the polarizing polarizing microscope, the following observations were made:
124
THE J0U1NAL Tfl1 JOURNALOF OFINVESTIGATIVE INVESTIGATIVEDEEMATOLOGY DERMATOLOGY
AN—
—AN
PD P0 FIG. 4. Horizontal section of human callus in polarized light showing circumferentially oriented oriented cornified cornified cells cells around around the the sweat sweat ducts. ducts. PU: PU: polarizer polarizer axis; axis; AN: AN: analyzer analyzer axis. axis.
Groove areas.—Each groove area showed maximal brightness if its longitudinal
axis was wasset settoto—45° 450 from from the polarizer axis (Fig. 3), indicating linear and axial orientation of keratin in these areas of the callus. callus. When When the the retardation retardation plate was inserted into the microscope and the longitudinal axis of groove areas was set to —45° (position shown in Fig. 3), each groove area showed a blue interference color, revealing positive sign of double refraction with reference to the longitudinal axis (compare with Fig. 1B). Consequently, it was concluded that in groove areas the long axis of chain molecules of keratin is preferentially oriented parallel to the longitudinal axis of grooves. Ridge areas.—In most sections, midway between neighboring sweat ducts, intensely birefringent cross-bands were seen connecting adjacent groove areas in a more or less transverse direction (Fig. 3). When the the retardation retardation plate plate was was inserted into the polarizing microscope, the cross-bands in the position shown
in Fig. 3 (oriented with the long axis at + 45°) showed a yellow subtraction color. This indicated that the preferential orientation of keratin chain molecules iii cross-band areas of the callus is transverse (compare Fig. 1C) and at right in angles to the chain molecules of groove areas. In a narrow region around the sweat ducts (Fig. 4), the single cornified cells showed positive index ellipsoids with long axes oriented circumferentially (Maltese cross) revealing an annularly oriented keratin structure. structure. Surrounding Surrounding the the sweat duct regions, a random orientation was seen roughly forming concentric rings.
ORIENTATION OF KERATIN KERATIN TN IN CORNIFIED CORNIFIED ET'ITHELIUM
125
DISCUSSION
Although x-ray analysis of hair, nail, and cormhed coriiihed epithelium of the skin shows that their structures are built up of similar aipha-keratin molecules (2, 3, 5), differences appear in the orientation of aipha-keratins alpha-keratins in the various horny tissues. Whereas in the hair and nail, orientation is linear, in thickened cornified epitheliurn a complex structure seems to prevail. The above observations indicate that the groove areas, together with cross-
band regions of ridge areas, form a lattice-like pattern in iii thickened cornified epitheliurn of the human skin. This lattice structure is schematically shown epithelium showii in iii Fig. 5. Functionally, the lattice structure may increase the mechanical strength of the cornified epithelium and assure isodimensional physical response to me-
Fi;. 5. Fie. 5. Schematic Schematic picture of oriented areas of human callus caIIu in in horizontal horizontal section. section.
chanical stress. The annular structure around the sweat ducts appears as an important support for the wall of the sweat duct and may assure its patency. SUMMARY
Polarization optical studies of serial sectioiis sections cut parallel to the surface of human callus showed that beneath the surface grooves, grooves, keratin keratin is is oriented oriented paralparallel to the surface plane and to the direction of the grooves. Beneath the ridges, a transverse orientation prevails, except in sweat duct regions which show an annularly oriented structure. The authors' sincere thanksarc aredue dueto toMrs. Mrs. Margit Margit Matolt.y Matoltsyfor forher hervaluable valuable assistance. assistance. ineere thanks
REFERENCES 1. Sciirsiiwr, ScHii1DT,W. W.J.: J.:Die DieBausteine Bausteinedes desTierkorpers Tierkörpersin inpolarisiertem polarisiertemLichte, Lichte,p. p.336. 336.Bonn, Bonn, Verlag von F. Cohen, 1924.
126
THE JOURNAL JOURNALOF OFINVESTIGATIVE INVESTIGATIVE DERMATOLOGY DERMATOLOGY
2. ASTBUEY, H. J.: J.: ASTBURY,W. W. T. T. AND AND Woons, Woons, H.
related fibers.
X-ray studies uf of the structure of hair, wool and
1934. A), 232: 333, A), 333, 1934. 3. J. C., HEEINGA,G. C.C. C.AND ANDWEIDINGER, WEIDINGER, A.: A.: On On keratin keratin and and cornification. cornification. 3.DEEK5EN, DIwcsiN, J. C.,HERINGA,
Phil. Tr. Roy. Soc. London, (Ser. (Ser.
Acta nccrl. neerl. Morphol., Morphol., 1: 1: 31, 31, 1937. DEEKsEN, C. AND ANDHERINGA, HERINGA,G. C.C.: C.:Verhornung Vcrhornungund undTonofibrillen Tonofibrillender derEpidermis. Epidermis. DERKSEN, J.J.C. Caz. lek., Gaz. lek., 15: 15: 532, 1936. 5. Cxuouo, A.AND AND CHAMPETIER, Recherches sur ics les roentgenogrammes roentgcnogrammes des kcratincs. CHAMPETIER, C.: Rccherches keratine. GIROUD,A. Bull. Soc. Soc. chim. chim. biol., 18: 656, 1936. 6. MATOLTsY, G.G.AND ANDODLAND, ODLAND,G.C.F.:F.:Tnvestigation Investigationof ofthe thestructure structure of of the the cornified cornificd MATOLTSY, A.A. epithelium cpithclium of of the the human human skin. skin. J. J. Biophysic. Biophysic. and and Biochem. Biochem. Cytol., Cytol., 1: 1: 191, 191, 1955. 1955. 7. BENNETT, H. S.: The microscopical investigation of biological materials with polarized 4. 4.
light. In TnMcClung's McClung'sHandbook Handbookof ofMicroscopical MicroscopicalTechnique Technique(H. (R.McClung McClungJones, Jones, Editor), p. 591. 591. New New York, York,Paul PaulB. B.Hoeber, Hoeber,Tnc., Inc., 1950. 1950.
DISCUSSION DR. FLESCH (Philadelphia, Penna.): I would DR. PETER PETER FLESCH (Philadelphia, Penna.): I would like like pointout outthat that totopoint such differences in keratin exist not only in calluses, but in normal epidermis. In an admirable work (Anat. Rec. 119: 449, 1954), it has been shown that different types of keratin occur on the skin of the finger tips and that these differences contribute to the tactile sensitivity. Da. VAN SCOTT Dn.EUGENE EUGENEJ. J. VAN SCOTT (Bethesda, Md.): I wouldlike liketotoask askDr. Dr.Matoltsy Matoltsy Md.): I would (Bethesda, what the anatomical relationship relatiollship of the sweat duct is to the dermal papilla. Dn. DR.A. A.GEDEON GEnEONMATOLTSY MATOLTSY closing): closing): WeWe have have studied studiedvery veryfew fewfull fullthickthick(in (in
ness skins by this method, so I don't think I can answer the question that Dr. Van Scott asks. asks. These These were were callus callussections sectionsand anddidn't didn'tcontain containany ay other part of the skin—only the cornified epithelium. epitheliurn.
THE JOURNAL OF INVESTIGATIVE DERMATOLOGY
94
linolenic acid extract. Arch. This pdf is a scanned copy UV of irradiated a printed document.
24. Wynn, C. H. and Iqbal, M.: Isolation of rat
skin lysosomes and a comparison with liver Path., 80: 91, 1965. and spleen lysosomes. Biochem. J., 98: lOP, 37. Nicolaides, N.: Lipids, membranes, and the 1966.
human epidermis, p. 511, The Epidermis
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