Evidence map›Paper›PMID 8267779›Full record

ArticleThe Journal of cell biology1993

Cell and heparin binding in the distal long arm of laminin: identification of active and cryptic sites with recombinant and hybrid glycoprotein.

U Sung, J J O'Rear, P D Yurchenco

Erratum issuedOpen access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Developing defined substrates for stem cell culture and differentiation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
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  16. Article
  17. Neuronal receptors mediating responses to antibodyactivated laminin-1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
  18. Review
  19. The alpha chain of laminin-1 is independently secreted and drives secretion of its beta- and gamma-chain partners.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

U SungDepartment of Pathology, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
J J O'Rear
P D Yurchenco
Johnson University · US

Funding

BASEMENT MEMBRANE SELF-ASSEMBLY &STRUCTURER01DK036425 · NIDDK · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI YURCHENCO, PETER DANA · 1986 to 2022
$4.3M
Basement Membrane Self-assembly and StructureR37DK036425 · NIDDK · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI YURCHENCO, PETER DANA · 2003 to 2012
$2.9M
NIDDK NIH HHS DK-36425
6 · The paper itself

Abstract

The long arm of laminin, which binds heparin and cells, consists of three polypeptides (A, B1, and B2) joined in a coiled-coil rod attached to a terminal A chain globule (G). Previously, we found that recombinant globular domain (rG) supported heparin and myoblast binding (Yurchenco, P. D., U. Sung, M. D. Ward, Y. Yamada, and J. J. O'Rear. 1993. J. Biol. Chem. 268:8356-8365). To further analyze long arm functions, we expressed the distal moiety of the mouse laminin A chain extending from the middle of the rod to the carboxyl terminus (rAiG). This larger glycoprotein, secreted by Sf9 insect cells infected with recombinant baculovirus, was intercalated in vitro into the corresponding disulfide-linked B chain segments of laminin fragment E8 (distal long arm rod and proximal globule). The hybrid molecule (B-rAiG) possessed a structure similar to laminin long arm as judged by electron microscopy and limited proteolysis. By joining rAiG with E8-B chains, the affinity of G domain for heparin decreased from that observed with rAiG and rG to one similar to native protein. HT1080 cells adhered to E8, rAiG, and B-rAiG, less well to rG, and not to denatured E8/B-rAiG, the A and B chain moieties of E8, or to a mixture of rG and E8-B chains. Cell adhesion to E8 and B-rAiG, in contrast to rAiG, was inhibited with antibodies specific for alpha 6 and beta 1 integrin chains. Since intercalation (a) restored a conformationally dependent alpha 6 beta 1 integrin recognition site present in native protein, (b) inactivated a cryptic cell binding activity in the A chain, and (c) inhibited a heparin binding site present in proximal G domain, we conclude that biological activities of laminin are different from that of its isolated subunits.

Indexed as

AnimalsCell AdhesionHeparinHumansLamininMiceModels, MolecularPancreatic ElastaseProtein BindingRecombinant Fusion ProteinsRecombinant ProteinsTumor Cells, CulturedHeparinLamininPancreatic ElastaseRecombinant Fusion ProteinsRecombinant Proteins

Identifiers

PMID8267779
PMCPMC2119876
OpenAlexW2289101943

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.