TY - JOUR
T1 - Isolation and characterization of a 30 kDa membrane glycoprotein from human stratum corneum
AU - Shu-Jen, Chen
AU - Rajaraman, Srinivasan
AU - Miller, Joanne
AU - Kalmaz, Gulgun D.
AU - Brysk, Miriam M.
N1 - Funding Information:
This investigation was supported by Grant Number CA 27441 from the National Cancer Institute and by Grant Number H-869 awarded from the Robert A. Welch Foundation to M.M.B. We want to thank Mr. Philip Penn for the im-munoelectron microscopy, Mrs. Freddie Williams for the immunofluorescence studies, and Mrs. Joy Rose for typing the manuscript.
PY - 1986/5/2
Y1 - 1986/5/2
N2 - Using iodinated concanavalin A in conjunction with gel electrophoresis, we have identified a 30 kDa glycoprotein in the stratum corneum of human skin. We isolated this glycoprotein by extraction in nonionic detergent, affinity chromatography and preparative gel electrophoresis. It binds to concanavalin A but not to three other lectins. The purified glycoprotein migrates at 30 kDa whether or not reducing agents are present. It is rich in histidine and lysine, but lacks arginine, proline, tyrosine and methionine. It is clearly distinct from fillaggrin. We prepared a monospecific polyclonal antibody to this glycoprotein and localized it by immuno-histochemistry exclusively to the cell membrane of corneocytes. We postulate that the glycoprotein may play a role in the cohesion and desquamation of corneocytes.
AB - Using iodinated concanavalin A in conjunction with gel electrophoresis, we have identified a 30 kDa glycoprotein in the stratum corneum of human skin. We isolated this glycoprotein by extraction in nonionic detergent, affinity chromatography and preparative gel electrophoresis. It binds to concanavalin A but not to three other lectins. The purified glycoprotein migrates at 30 kDa whether or not reducing agents are present. It is rich in histidine and lysine, but lacks arginine, proline, tyrosine and methionine. It is clearly distinct from fillaggrin. We prepared a monospecific polyclonal antibody to this glycoprotein and localized it by immuno-histochemistry exclusively to the cell membrane of corneocytes. We postulate that the glycoprotein may play a role in the cohesion and desquamation of corneocytes.
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U2 - 10.1016/0304-4165(86)90029-2
DO - 10.1016/0304-4165(86)90029-2
M3 - Article
C2 - 3083868
AN - SCOPUS:0022460767
SN - 0304-4165
VL - 881
SP - 375
EP - 382
JO - BBA - General Subjects
JF - BBA - General Subjects
IS - 3
ER -