GLYCAM1

{{protein

|Name=glycosylation dependent cell adhesion molecule-1

|caption=

|image=

|width=

|HGNCid=18023

|Symbol=GLYCAM1

|AltSymbols=

|EntrezGene=644076

|OMIM=

|RefSeq=XM_927461

|UniProt=Q8IVK1

|PDB=

|ECnumber=

|Chromosome=12

|Arm=q

|Band=13.2

|LocusSupplementaryData=

}}

Glycosylation-dependent cell adhesion molecule-1 (GLYCAM1) is a proteoglycan ligand expressed on cells of the high endothelial venules in lymphoid tissues. It is the ligand for the receptor L-selectin allowing for naive lymphocytes to exit the bloodstream into lymphoid tissues.{{Cite book|title=Leukocyte Migration and Adhesion|volume=58|last1=Imhof|first1=Beat A.|last2=Dunon|first2=Dominique|pages=345–416|doi=10.1016/s0065-2776(08)60623-9|series=Advances in Immunology|year=1995|pmid=7537936|isbn=9780120224586|url-access=registration|url=https://archive.org/details/advancesinimmuno58dixo/page/345}}{{Cite journal|last2=Kraal|first2=G.|last3=Mebius|first3=R. E.|last4=Watson|first4=S. R.|date=1 November 1992|title=Identification of a soluble form of a ligand for the lymphocyte homing receptor|pmc=2119429|journal=The Journal of Experimental Medicine|volume=176|issue=5|pages=1415–1419|pmid=1383387|doi=10.1084/jem.176.5.1415|last1=Brustein|first1=M.}}

GLYCAM1 binds to L-selectin by presenting one or more O-linked carbohydrates to the lectin domain of the leukocyte cell surface selectin.{{citation needed|date=May 2016}}

Data suggests that GLYCAM1 is a hormone-regulated milk protein that is part of the milk mucin complex.{{cite journal | vauthors = Dowbenko D, Kikuta A, Fennie C, Gillett N, Lasky LA | title = Glycosylation-dependent cell adhesion molecule 1 (GlyCAM 1) mucin is expressed by lactating mammary gland epithelial cells and is present in milk | journal = The Journal of Clinical Investigation | volume = 92 | issue = 2 | pages = 952–60 | date = August 1993 | pmid = 8349827 | pmc = 294935 | doi = 10.1172/JCI116671 }}

GlyCAM-1 is expressed exclusively on high endothelial venules. It is unclear how GlyCAM-1 is attached to the membrane as it lacks a transmembrane region.