Isolation and characterization of mouse CD7 cDNA View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-01

AUTHORS

Kazuhiro Yoshikawa, Masao Seto, Ryuzo Ueda, Yuichi Obata, Hidetoshi Fukatsu, Kaio Segawa, Toshitada Takahashi

ABSTRACT

The human CD7 antigen is a glycoprotein, Mr40 000, expressed on the surface of peripheral blood T-lymphocytes and thymocytes, and is the earliest surface antigen to appear on T-cell lineage cells. In this study, putative mouse CD7 cDNA was identified based on its similarities with human CD7. Five independent clones originating from the same mRNA species were isolated (designated as mCD7) by screening a mouse thymocyte cDNA library with human CD7 cDNA, J61, under moderate stringency. The longest insert of a 995 base pair had an open reading frame of 210 amino acids. Northern blot analysis using the mouse CD7 cDNA probe demonstrated a single 1.2 kilobase mRNA ni the thymus, spleen, bone marrow, and small intestine. The protein deduced from mCD7 cDNA consisted of the leader, extracellular, transmembrane, and cytoplasmic domains of 24, 126, 21, and 39 amino acids, respectively, based on the hydrophobicity plot and the structure of human CD7. The extracellualr domain contained three potential N-glycosilation sites, while the cytoplasmic domain contained one potential protein kinase C phosphorylation site. The amino acid sequence had 45.5% similarity with human CD7, while the similarities for the individual domains ranged from 49.2% to 63.2%. The six highly conserved regions, which may possibly be involved with still unknown CD7-mediated functions, were located in the extracellular and cytoplasmic domains. More... »

PAGES

114-119

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00216834

DOI

http://dx.doi.org/10.1007/bf00216834

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045411959

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7678579


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