About: Human Mig chemokine: biochemical and functional characterization

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About: Human Mig chemokine: biochemical and functional characterization Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Human Mig chemokine: biochemical and functional characterization
Creator	Liao, Fang Rabin, Ronald Farber, Joshua Koniaris, Leonidas Yannelli, John
topic	covid:daf06fe518af2567566bd71fca278c8bc5fecddf#this
Source	PMC
abstract	Mig is a chemokine of the CXC subfamily that was discovered by differential screening of a cDNA library prepared from lymphokine- activated macrophages. The mig gene is inducible in macrophages and in other cells in response to interferon (IFN)-gamma. We have transfected Chinese hamster ovary (CHO) cells with cDNA encoding human Mig and we have derived CHO cell lines from which we have purified recombinant human Mig (rHuMig). rHuMig induced the transient elevation of [Ca2+]i in human tumor-infiltrating T lymphocytes (TIL) and in cultured, activated human peripheral blood-derived lymphocytes. No responses were seen in human neutrophils, monocytes, or Epstein-Barr virus-transformed B lymphoblastoid cell lines. rHuMig was chemotactic for TIL by a modified Boyden chamber assay but rHuMig was not chemotactic for neutrophils or monocytes. The CHO cell lines, IFN-gamma-treated human peripheral-blood monocytes, and IFN-gamma-treated cells of the human monocytic cell line THP-1 all secreted multiple and identical HuMig species as revealed by SDS-PAGE. Using the CHO-derived rHuMig, we have shown that the species' heterogeneity is due to proteolytic cleavage at basic carboxy-terminal residues, and that the proteolysis occurs before and not after rHuMig secretion by the CHO cells. The major species of secreted rHuMig ranged from 78 to 103 amino acids in length, the latter corresponding to the full-length secreted protein predicted from the HuMig cDNA. Carboxy-terminal-truncated forms of rHuMig were of lower specific activity compared to full-length rHuMig in the calcium flux assay, and the truncated species did not block the activity of the full- length species. It is likely that HuMig plays a role in T cell trafficking and perhaps in other aspects of the physiology of activated T cells.
has issue date	1995-11-01(xsd:dateTime)
bibo:pmid	7595201
has license	cc-by-nc-sa
sha1sum (hex)	daf06fe518af2567566bd71fca278c8bc5fecddf
resource representing a document's title	Human Mig chemokine: biochemical and functional characterization
has PubMed Central identifier	PMC2192190
has PubMed identifier	7595201
schema:publication	J Exp Med
resource representing a document's body	covid:daf06fe518af2567566bd71fca278c8bc5fecddf#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/daf06fe518af2567566bd71fca278c8bc5fecddf
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