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Association of wild type and structurally modified epidermal growth factor receptors with the cytoskeleton
Growth factors and their receptors (78-110)
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EXPRESSION OF NGF RECEPTOR MRNA IN RODENT TESTIS UNDER NORMAL AND EXPERIMENTAL CONDITIONS. C. AYER-LELIEVRE1,2 M.J. VILLAR 2, O. SODER3, L, OLSON2~T. H01~'~:LT2 AND H. PERSSON1 Departments of Molecular Neurobiology1, Histology & Neurobiology2, Pediatrics & DevelopmentalEndocrinology3, KarolinskaInstitute, PO Box 60400, S-10401, Stockholm, Sweden. Nerve growth factor (NGF) is synthesized in germ cells of rat and mouse testis.* So far, the role for NGF in the male reproductive system is unknown. We have now investigated the presence and distribution of NGF receptor (NGFR) mRNA in testis using both RNA blot and in situ hybridization techniques. NGFR mRNA was detected in testis of both rat and mouse although at higher levels in mouse glands. The distribution and basal location of the hybridizing cells in the seminiferous epithelium suggest the synthesis of NGFR by Sertoli cells. The levels of NGFR mRNA were altered under experimental conditions which resulted in disappearance of NGF-producing germ cells. These observations support the hypothesis of a role for NGFR in spermatogenesis. *Ayer-LeLievre et al., PNAS 85, 2628, 1988.
A S S O C I A T I O N OF WILD TYPE AND S T R U C T U R A L L Y M O D I F I E D E P I D E R M A L G R O W T H FACTOR RECEPTORS WITH THE C Y T O S K E L E T O N N van Belzen, AJ Verkleij, and J B o o n s t r a Dept. of M o l e c u l a r Cell Biology, U n i v e r s i t y of Utrecht, 3584 CH Utrecht, The N e t h e r l a n d s Using NIH-3T3 mouse cells t r a n s f e c t e d with human e p i d e r m a l growth factor receptor (EGFR) cDNA, we studied the interaction of structurally m o d i f i e d EGFRs with the cytoskeleton. In E G F - t r e a t e d cells e x p r e s s i n g wild type EGFRs, part of the E G F R p o p u l a t i o n was associated with the cytoskeleton. EGFR constructs w h i c h d i s p l a y e d no kinase activity due to the r e p l a c e m e n t of lys721 by ala721, r e s e m b l e d w i l d type receptors with respect to their a s s o c i a t i o n with the cytoskeleton. Similarly, EGFRs from which the 126 C-terminal amino acids had been d e l e t e d were capable to interact w i t h c y t o s k e l e t a l elements. We conclude that the kinase a c t i v i t y and the amino acid residues 1061-1186 of the EGFR are not involved in its a s s o c i a t i o n with the cytoskeleton. ACKNOWLEDGEMENTS We t h a n k Dr. J. S c h l e s s i n g e r for p r o v i d i n g the t r a n s f e c t e d cell lines. This w o r k was supported by B I O N / N W O grant no. 417.18.
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EXPRESSION OF NGF RECEPTOR MRNA IN RODENT TESTIS UNDER NORMAL AND EXPERIMENTAL CONDITIONS. C. AYER-LELIEVRE1,2 M.J. VILLAR 2, O. SODER3, L, OLSON2~T. H01~'~:LT2 AND H. PERSSON1 Departments of Molecular Neurobiology1, Histology & Neurobiology2, Pediatrics & DevelopmentalEndocrinology3, KarolinskaInstitute, PO Box 60400, S-10401, Stockholm, Sweden. Nerve growth factor (NGF) is synthesized in germ cells of rat and mouse testis.* So far, the role for NGF in the male reproductive system is unknown. We have now investigated the presence and distribution of NGF receptor (NGFR) mRNA in testis using both RNA blot and in situ hybridization techniques. NGFR mRNA was detected in testis of both rat and mouse although at higher levels in mouse glands. The distribution and basal location of the hybridizing cells in the seminiferous epithelium suggest the synthesis of NGFR by Sertoli cells. The levels of NGFR mRNA were altered under experimental conditions which resulted in disappearance of NGF-producing germ cells. These observations support the hypothesis of a role for NGFR in spermatogenesis. *Ayer-LeLievre et al., PNAS 85, 2628, 1988.
A S S O C I A T I O N OF WILD TYPE AND S T R U C T U R A L L Y M O D I F I E D E P I D E R M A L G R O W T H FACTOR RECEPTORS WITH THE C Y T O S K E L E T O N N van Belzen, AJ Verkleij, and J B o o n s t r a Dept. of M o l e c u l a r Cell Biology, U n i v e r s i t y of Utrecht, 3584 CH Utrecht, The N e t h e r l a n d s Using NIH-3T3 mouse cells t r a n s f e c t e d with human e p i d e r m a l growth factor receptor (EGFR) cDNA, we studied the interaction of structurally m o d i f i e d EGFRs with the cytoskeleton. In E G F - t r e a t e d cells e x p r e s s i n g wild type EGFRs, part of the E G F R p o p u l a t i o n was associated with the cytoskeleton. EGFR constructs w h i c h d i s p l a y e d no kinase activity due to the r e p l a c e m e n t of lys721 by ala721, r e s e m b l e d w i l d type receptors with respect to their a s s o c i a t i o n with the cytoskeleton. Similarly, EGFRs from which the 126 C-terminal amino acids had been d e l e t e d were capable to interact w i t h c y t o s k e l e t a l elements. We conclude that the kinase a c t i v i t y and the amino acid residues 1061-1186 of the EGFR are not involved in its a s s o c i a t i o n with the cytoskeleton. ACKNOWLEDGEMENTS We t h a n k Dr. J. S c h l e s s i n g e r for p r o v i d i n g the t r a n s f e c t e d cell lines. This w o r k was supported by B I O N / N W O grant no. 417.18.
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