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PMID: 2628733 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Human transforming growth factor-beta 3: recombinant expression, purification, and biological activities in comparison with transforming growth factors-beta 1 and -beta 2.

Molecular endocrinology (Baltimore, Md.) ·Vol. 3 ·No. 12 ·1989-12-00 ·Pages 1977-86

Graycar JL, Miller DA, Arrick BA, Lyons RM, Moses HL, Derynck R

Abstract

Recent cDNA characterization has predicted the existence of a new member of the transforming growth factor family, transforming growth factor-beta 3 (TGF beta 3). However, nothing is known about the biological activities of the TGF beta 3 protein, since it has not been purified from any natural sources. We report here the recombinant expression in mammalian cells and the purification to apparent homogeneity of human TGF beta 3. The TGF beta 3 was evaluated in comparison with purified TGF beta 1 and TGF beta 2 in several assays for its effects on stimulation or inhibition of proliferation of mammalian cells. These analyses revealed that TGF beta 3 exerts activities similar to the two other TGF beta species, but that there are distinct differences in potencies between the different TGF beta forms depending on the cell type and assay used.

MeSH Terms
Animals Cell Division/drug effects Cell Line Cricetinae DNA/biosynthesis Gene Expression Genes Humans Recombinant Proteins/biosynthesis Transforming Growth Factors/biosynthesis,genetics
Chemicals
Recombinant Proteins Transforming Growth Factors DNA
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Graycar J L
Department of Developmental Biology, Genentech, Inc. South San Francisco, California 94080.
Miller D A
Arrick B A
Lyons R M
Moses H L
Derynck R
Article Info
Journal
Molecular endocrinology (Baltimore, Md.)
Abbr.
Mol Endocrinol
ISSN
0888-8809
Published
1989-12-00
Pages
1977-86
Language
English
Region
United States
NLM ID
8801431
Subset
IM
Grants
NCI NIH HHS · CA-42572 · United States
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