HCC-2, a human chemokine: Gene structure, expression pattern, and biological activity

Cloning and sequencing of the upstream region of the gene of the CC chemokine HCC-1 led to the discovery of an adjacent gene coding for a CC chemokine that was named “HCC-2.” The two genes are separated by 12-kbp and reside in a head-to-tail orientation on chromosome 17. At variance with the genes f...

ver descrição completa

Na minha lista:
Detalhes bibliográficos
Main Authors: Pardigol, Andreas, Forssmann, Ulf, Zucht, Hans-Dieter, Loetscher, Pius, Schulz-Knappe, Peter, Baggiolini, Marco, Forssmann, Wolf-Georg, Mägert, Hans-Jürgen
Formato: Artigo
Idioma:en
Publicado em: The National Academy of Sciences 1998
Assuntos:
Biological Sciences
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC27666/
https://ncbi.nlm.nih.gov/pubmed/9600961
Tags: Adicionar Tag
Sem tags, seja o primeiro a adicionar uma tag!
id pubmed-27666
record_format dspace
spelling pubmed-276662001-03-17 HCC-2, a human chemokine: Gene structure, expression pattern, and biological activity Pardigol, Andreas Forssmann, Ulf Zucht, Hans-Dieter Loetscher, Pius Schulz-Knappe, Peter Baggiolini, Marco Forssmann, Wolf-Georg Mägert, Hans-Jürgen Proc Natl Acad Sci U S A Biological Sciences Cloning and sequencing of the upstream region of the gene of the CC chemokine HCC-1 led to the discovery of an adjacent gene coding for a CC chemokine that was named “HCC-2.” The two genes are separated by 12-kbp and reside in a head-to-tail orientation on chromosome 17. At variance with the genes for HCC-1 and other human CC chemokines, which have a three-exon-two-intron structure, the HCC-2 gene consists of four exons and three introns. Expression of HCC-2 and HCC-1 as studied by Northern analysis revealed, in addition to the regular, monocistronic mRNAs, a common, bicistronic transcript. In contrast to HCC-1, which is expressed constitutively in numerous human tissues, HCC-2 is expressed only in the gut and the liver. HCC-2 shares significant sequence homology with CKβ8 and the murine chemokines C10, CCF18/MRP-2, and macrophage inflammatory protein 1γ, which all contain six instead of four conserved cysteines. The two additional cysteines of HCC-2 form a third disulfide bond, which anchors the COOH-terminal domain to the core of the molecule. Highly purified recombinant HCC-2 was tested on neutrophils, eosinophils, monocytes, and lymphocytes and was found to exhibit marked functional similarities to macrophage inflammatory protein 1α. It is a potent chemoattractant and inducer of enzyme release in monocytes and a moderately active attractant for eosinophils. Desensitization studies indicate that HCC-2 acts mainly via CC chemokine receptor CCR1. The National Academy of Sciences 1998-05-26 /pmc/articles/PMC27666/ /pubmed/9600961 Text en Copyright © 1998, The National Academy of Sciences
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Biological Sciences
spellingShingle Biological Sciences
Pardigol, Andreas
Forssmann, Ulf
Zucht, Hans-Dieter
Loetscher, Pius
Schulz-Knappe, Peter
Baggiolini, Marco
Forssmann, Wolf-Georg
Mägert, Hans-Jürgen
HCC-2, a human chemokine: Gene structure, expression pattern, and biological activity
description Cloning and sequencing of the upstream region of the gene of the CC chemokine HCC-1 led to the discovery of an adjacent gene coding for a CC chemokine that was named “HCC-2.” The two genes are separated by 12-kbp and reside in a head-to-tail orientation on chromosome 17. At variance with the genes for HCC-1 and other human CC chemokines, which have a three-exon-two-intron structure, the HCC-2 gene consists of four exons and three introns. Expression of HCC-2 and HCC-1 as studied by Northern analysis revealed, in addition to the regular, monocistronic mRNAs, a common, bicistronic transcript. In contrast to HCC-1, which is expressed constitutively in numerous human tissues, HCC-2 is expressed only in the gut and the liver. HCC-2 shares significant sequence homology with CKβ8 and the murine chemokines C10, CCF18/MRP-2, and macrophage inflammatory protein 1γ, which all contain six instead of four conserved cysteines. The two additional cysteines of HCC-2 form a third disulfide bond, which anchors the COOH-terminal domain to the core of the molecule. Highly purified recombinant HCC-2 was tested on neutrophils, eosinophils, monocytes, and lymphocytes and was found to exhibit marked functional similarities to macrophage inflammatory protein 1α. It is a potent chemoattractant and inducer of enzyme release in monocytes and a moderately active attractant for eosinophils. Desensitization studies indicate that HCC-2 acts mainly via CC chemokine receptor CCR1.
author Pardigol, Andreas
Forssmann, Ulf
Zucht, Hans-Dieter
Loetscher, Pius
Schulz-Knappe, Peter
Baggiolini, Marco
Forssmann, Wolf-Georg
Mägert, Hans-Jürgen
author_facet Pardigol, Andreas
Forssmann, Ulf
Zucht, Hans-Dieter
Loetscher, Pius
Schulz-Knappe, Peter
Baggiolini, Marco
Forssmann, Wolf-Georg
Mägert, Hans-Jürgen
author_sort Pardigol, Andreas
title HCC-2, a human chemokine: Gene structure, expression pattern, and biological activity
title_short HCC-2, a human chemokine: Gene structure, expression pattern, and biological activity
title_full HCC-2, a human chemokine: Gene structure, expression pattern, and biological activity
title_fullStr HCC-2, a human chemokine: Gene structure, expression pattern, and biological activity
title_full_unstemmed HCC-2, a human chemokine: Gene structure, expression pattern, and biological activity
title_sort hcc-2, a human chemokine: gene structure, expression pattern, and biological activity
publisher The National Academy of Sciences
publisher_facet The National Academy of Sciences
publishDate 1998
url https://ncbi.nlm.nih.gov/pmc/articles/PMC27666/
https://ncbi.nlm.nih.gov/pubmed/9600961
_version_ 1758993821711990784

Registos relacionados