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A collagen-binding protein involved in the differentiation of myoblasts recognizes the Arg-Gly-Asp sequence.

Abstract：

:We had earlier demonstrated that a 46-kDa glycoprotein is involved in the differentiation of rat skeletal myoblasts. We now show that the binding of this glycoprotein to collagen and gelatin is disrupted by Arg-Gly-Asp (RGD) containing peptide but not by Arg-Gly-Glu (RGE). The former peptide also selectively elutes the 46-kDa glycoprotein bound to gelatin-Sepharose. Since all other proteins which bind RGD sequences have been found at the cell surface, we attempted to localize the 46-kDa glycoprotein by means of immuno fluorescent staining and radioiodine labeling. Surprisingly, the majority of the protein was found to be localized in the endoplasmic reticulum. Protease treatment of a microsomal fraction revealed that the protein is in the interior of the reticulum. Immunoprecipitation experiments, using a polyclonal antibody against the 46-kDa protein, demonstrated that no closely related proteins exist in myoblasts and also confirmed that the protein was not a fragment of a cell-surface localized protein. These findings suggest that the RGD sequence is also used in protein recognition within the cell.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Nandan D,Cates GA,Ball EH,Sanwal BD

doi

10.1016/0014-4827(88)90368-0

subject

Has Abstract

pub_date

1988-11-01 00:00:00

pages

289-97

issue

1

eissn

0014-4827

issn

1090-2422

pii

0014-4827(88)90368-0

journal_volume

179

pub_type

杂志文章

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