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B-galactoside-binding lectin of human and bovine tissues
Cell Biology
International
Reports, Vol. 4, No. 8, August
In recmtms a f&ily of B-gslactoside binding lecuns have teendescribed ins nmber of vertebrate ttssws(revierad in r&.8&9). l’hsselsctim differ frmthemenbrsm sssmistd hepauc biding glycoprotein’ in that they occur in katerso1uble as lF2l.l. as malbre asscciatal form; they are oflmrmleculsr wight,are em ard are thio1-rlxiwil?g divalent catim irde !? gro~requfring 2A . i%scleisarichsource of tbese1ectfns ard amngtte best characterized sreu-loseisOlstedfmcalflT%srt2-5and chick skeletalmscle 7. hk IEwe previously czh3wlthat there is considerable aTlug& similarity b&em the B-gal&c&de binding lectinsofhmw,mmkey~bovine~cles4 sqz&est~tbsttbeselectimhwebeenconselval through evolution. Us* rabbit antisera sgainstbmine hxrt ard hIam Ekeletal lnlscle k&ins w! twJe pzrformi indirect immmfluoresceKle sld jnlmlmperoxidase
775
1980
experimmtswithcryostatsectionsoftmrt, skeletal ad enoothIrmscles. lk results imlicate thsttbelectinistmkminmtlyexrracellular, associatslwithtk mrfscemmbr~ofmscle oells, in the carnective tissue cells and in endothelial 4.k 0f capillaries (~ig.~). in addition there is evidence for tlx preseme of 1ectin or antig-y indisti~shable substance in mmy other tissues. With one potentsntisenmsgsfnstbwim Imrtlectin irnmm-fluorescence kes observed in cryustat sections of nwlei (Fig.B). Sections of mclei &elesls,shmltDstsinnpmth.?sdditionof fluorescein-calj bovine serm albunin derivatfzedwithlactose residues(BsA-lactos&. Thisstainirgcouldhfnbibiteddtbnorr fluxescent ESA-lactose but rot with BSAderivatized withlrlsmmJs2residues. Further imestigatiom sre required to amfirm th.3 presence ofgslsctosebirdirglectin innuclei.
Mirect immmfluxescent staining of calf-tissue sectiom with F(sb’)2 fragnents of cm ;ntiserm to calf lesrt lectin (insets F(ab’)2 frqnents of mmzal rabbit senm). (A) Skeletal mscle showing stsiniq at periphery of fibres srd interstitial tissues. (B)Pancreas slxmirgcyimplsmicsswllas dear flImmfl.mrescence. 1. klwzll, G. and Rae, T. (1978) In Wthods in i?nqmlogy. Vol. L. Cw%ohydrates. Part C., V. Ginsburg, editor. Acad& Press, NewYork, p. 287-288. 2. Briles, E.B., Gregory, W., Fletcher, P. snd Komfcld, S. (1979) J. Cell Biol. & 528-537. 3. Childs, R.A. and F&xi, T. (1979) F&s. Letts. 3, 175-179. 4. &ilds. R.A. and Feid. T. (1979) Bioctrm. J.183, 755-758. 5. De Wsani. A., Hi&mm. S. ard Km&M, S.(1976) J. Biol. f&m. 251, 7581-7587. 6. Kim&, C., k&e, AX., Ddmtte, F. snd Kmsigny, M. (1979) F&s. J..etts.~, 329-332. 7. Kobikr, D., Beyer, E.C. and Bsrord~, S.H. (1978) DeveLop. Biol. 64, 265-272. 8. SimFson, D.L., =m% D.R. and Ioh, UH. (1978) Life Sciences, 22, 727-748, 9. Teichberg, V.I. (1978) In&tin Ruqmology. Vol. L. Carkobydrates. Part C., V.Gin&urg, editor. Acadentc Press, NewYork, p. 291-302.
01980Academic
Press Inc. (London!
Ltd.
International
Reports, Vol. 4, No. 8, August
In recmtms a f&ily of B-gslactoside binding lecuns have teendescribed ins nmber of vertebrate ttssws(revierad in r&.8&9). l’hsselsctim differ frmthemenbrsm sssmistd hepauc biding glycoprotein’ in that they occur in katerso1uble as lF2l.l. as malbre asscciatal form; they are oflmrmleculsr wight,are em ard are thio1-rlxiwil?g divalent catim irde !? gro~requfring 2A . i%scleisarichsource of tbese1ectfns ard amngtte best characterized sreu-loseisOlstedfmcalflT%srt2-5and chick skeletalmscle 7. hk IEwe previously czh3wlthat there is considerable aTlug& similarity b&em the B-gal&c&de binding lectinsofhmw,mmkey~bovine~cles4 sqz&est~tbsttbeselectimhwebeenconselval through evolution. Us* rabbit antisera sgainstbmine hxrt ard hIam Ekeletal lnlscle k&ins w! twJe pzrformi indirect immmfluoresceKle sld jnlmlmperoxidase
775
1980
experimmtswithcryostatsectionsoftmrt, skeletal ad enoothIrmscles. lk results imlicate thsttbelectinistmkminmtlyexrracellular, associatslwithtk mrfscemmbr~ofmscle oells, in the carnective tissue cells and in endothelial 4.k 0f capillaries (~ig.~). in addition there is evidence for tlx preseme of 1ectin or antig-y indisti~shable substance in mmy other tissues. With one potentsntisenmsgsfnstbwim Imrtlectin irnmm-fluorescence kes observed in cryustat sections of nwlei (Fig.B). Sections of mclei &elesls,shmltDstsinnpmth.?sdditionof fluorescein-calj bovine serm albunin derivatfzedwithlactose residues(BsA-lactos&. Thisstainirgcouldhfnbibiteddtbnorr fluxescent ESA-lactose but rot with BSAderivatized withlrlsmmJs2residues. Further imestigatiom sre required to amfirm th.3 presence ofgslsctosebirdirglectin innuclei.
Mirect immmfluxescent staining of calf-tissue sectiom with F(sb’)2 fragnents of cm ;ntiserm to calf lesrt lectin (insets F(ab’)2 frqnents of mmzal rabbit senm). (A) Skeletal mscle showing stsiniq at periphery of fibres srd interstitial tissues. (B)Pancreas slxmirgcyimplsmicsswllas dear flImmfl.mrescence. 1. klwzll, G. and Rae, T. (1978) In Wthods in i?nqmlogy. Vol. L. Cw%ohydrates. Part C., V. Ginsburg, editor. Acad& Press, NewYork, p. 287-288. 2. Briles, E.B., Gregory, W., Fletcher, P. snd Komfcld, S. (1979) J. Cell Biol. & 528-537. 3. Childs, R.A. and F&xi, T. (1979) F&s. Letts. 3, 175-179. 4. &ilds. R.A. and Feid. T. (1979) Bioctrm. J.183, 755-758. 5. De Wsani. A., Hi&mm. S. ard Km&M, S.(1976) J. Biol. f&m. 251, 7581-7587. 6. Kim&, C., k&e, AX., Ddmtte, F. snd Kmsigny, M. (1979) F&s. J..etts.~, 329-332. 7. Kobikr, D., Beyer, E.C. and Bsrord~, S.H. (1978) DeveLop. Biol. 64, 265-272. 8. SimFson, D.L., =m% D.R. and Ioh, UH. (1978) Life Sciences, 22, 727-748, 9. Teichberg, V.I. (1978) In&tin Ruqmology. Vol. L. Carkobydrates. Part C., V.Gin&urg, editor. Acadentc Press, NewYork, p. 291-302.
01980Academic
Press Inc. (London!
Ltd.