Publication Date:
1979-06-22
Description:
The pentapeptide arginyl-lysyl-aspartyl-valyl-tyrosine, corresponding to amino acid residues 32--36 in thymopoietin, was synthesized. In vitro, this pentapeptide induced the differentiation of murine prothymocytes to thymocytes and inhibited differentiative induction of cells of the B lineage. This combination of actions is presently unique to the parent molecule thymopoietin. In vivo, the pentapeptide reduced the high numbers of autologous rosette-forming cells normally present in the spleens of athymic mice; this also is a property of thymopoietin. These results suggest that this readily synthesized pentapeptide corresponds to an active site of thymopoietin and might serve as a therapeutic substitute for thymopoietin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldstein, G -- Scheid, M P -- Boyse, E A -- Schlesinger, D H -- Van Wauwe, J -- New York, N.Y. -- Science. 1979 Jun 22;204(4399):1309-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/451537" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Antigens, Surface/analysis
;
Cell Differentiation/drug effects
;
Complement System Proteins
;
Isoantigens/analysis
;
Lymphocytes/cytology/*immunology
;
Mice
;
Mice, Nude/immunology
;
Oligopeptides/chemical synthesis/*pharmacology
;
Receptors, Drug/analysis
;
Structure-Activity Relationship
;
Thymopoietins/*pharmacology
;
Thymus Hormones/*pharmacology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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