LAMC2

Official Full Name

laminin subunit gamma 2

Organism

Homo sapiens

GeneID

3918

Background

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins, composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively), have a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 2. The gamma 2 chain, formerly thought to be a truncated version of beta chain (B2t), is highly homologous to the gamma 1 chain; however, it lacks domain VI, and domains V, IV and III are shorter. It is expressed in several fetal tissues but differently from gamma 1, and is specifically localized to epithelial cells in skin, lung and kidney. The gamma 2 chain together with alpha 3 and beta 3 chains constitute laminin 5 (earlier known as kalinin), which is an integral part of the anchoring filaments that connect epithelial cells to the underlying basement membrane. The epithelium-specific expression of the gamma 2 chain implied its role as an epithelium attachment molecule, and mutations in this gene have been associated with junctional epidermolysis bullosa, a skin disease characterized by blisters due to disruption of the epidermal-dermal junction. Two transcript variants resulting from alternative splicing of the 3' terminal exon, and encoding different isoforms of gamma 2 chain, have been described. The two variants are differentially expressed in embryonic tissues, however, the biological significance of the two forms is not known. Transcript variants utilizing alternative polyA_signal have also been noted in literature. [provided by RefSeq, Aug 2011]

Synonyms

B2T; CSF; EBR2; BM600; EBR2A; JEB3A; JEB3B; LAMB2T; LAMNB2;

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Detailed Information

Recent Progress

Laminins are crucial proteins in the basal lamina, and these form a protein network that influences both normal and transformed cell differentiation, migration and adhesion, as well as phenotype and survival. Several studies in cancers have shown that the elevated expression of LAMC2 on cancer cells appears to drive tumorigenesis through its interactions with several cell-surface receptors including several integrins and EGFRs. Accumulating evidence indicated that LAMC2-mediated signaling network plays an important role in the progression, migration and invasion of multiple types of cancer, suggesting that it might be a potential therapeutic anticancer target for inhibiting tumorigenesis. Furthermore, elevated serum levels of LAMC2 in cancer patients might appear as attractive serum-based diagnostic biomarker.

Fig. 1. Schematic illustrations of Laminin-332 structure: Laminin-332 forms a cruciform shaped structure consisting of three chains (alpha3, beta3 and gamma2, also known as LAMC2). (Garg et al, 2014)

It is universally acknowledged that lung cancer is the number one cancer killer, and metastasis is the main cause of high mortality in lung cancer patients. Researchers identified LAMC2 to be significantly upregulated in lung adenocarcinoma metastatic cells. Elevated LAMC2 increased traction force, migration, and invasion of lung adenocarcinoma cells accompanied by the induction of epithelial-mesenchymal transition (EMT), while LAMC2 knockdown decreased traction force, migration, and invasion accompanied by EMT reduction in vitro, along with attenuated metastasis in mice. High LAMC2 was significantly correlated with the mesenchymal marker vimentin expression in lung adenocarcinomas, and with higher risk of recurrence or death in patients with lung adenocarcinoma. These findings, taken together, suggested that LAMC2 may promote metastasis in lung adenocarcinoma via EMT and could be a potential therapeutic target.

In another study, given that non-small cell lung cancer (NSCLC) lacks reliable serological biomarkers for predicting patients' survival and response to treatment, researchers conducted a study to examine the capability of serum LAMC2 and four known tumor markers for disease prognosis and patients' risk stratification. LAMC2, CA 125, CEA, CYFRA 21-1 and SCC levels were retrospectively measured. LAMC2 showed significant prognostic ability for overall survival in the full cohort. LAMC2 and CYFRA 21-1 combination enhanced prognostic models based on common clinical parameters, further enabling stratification of patients into clear risk groups. Thus this study indicated LAMC2 as a novel NSCLC prognostic factor. LAMC2 combined with CA 125 and CYFRA 21-1 could aid in clinical prediction of NSCLC patients' overall survival and inform clinical practice.

In search of the effective diagnostic, prognostic and disease-monitoring biomarkers for pancreatic ductal adenocarcinoma (PDAC), researchers identified a total of 2,190 non-redundant proteins in four PDAC tissues and their adjacent benign tissues. results showed a significant elevation of LAMC2 in pancreatic cancer serum. Extensive validation of LAMC2 in healthy, benign, and PDAC sera from geographically diverse cohorts demonstrated a significant increase in levels in early-stage PDAC compared to benign diseases. The combination of LAMC2 and CA19.9 improved the individual diagnostic performance in distinguishing healthy and benign subjects from PDAC. Additionally, LAMC2 was positive in about 60% of patients with PDAC who had no CA19.9 elevation. Thus it was concluded that LAMC2 is a new serum biomarker for pancreatic adenocarcinoma.

To evaluate the effects of SNPs (single nucleotide polymorphisms) on CRC (colorectal cancer) susceptibility in Chinese populations, researchers screened out all potentially functional SNPs in exons of lncRNAs (long non-coding RNA) located in CRC susceptibility loci. Analysis showed that CG and GG genotypes of the rs2147578 were significantly associated with increased risk for CRC occurrence. Bioinformatics analyses showed that rs2147578 is located in the transcript of lnc-LAMC2-1:1 and could influence the binding of lnc-LAMC2-1:1/miR-128-3p. Further analysis showed that rs2147578 is correlated with the expression of a well-established oncogene LAMC2. These findings indicated that rs2147578 in lnc-LAMC2-1:1 might be a genetic modifier for the development of CRC.

References:

Garg, M., Braunstein, G., & Koeffler, H. P. (2014). Lamc2 as a therapeutic target for cancers. Expert Opinion on Therapeutic Targets, 18(9), 979-82.
Moon, Y. W., Rao, G., Kim, J. J., Shim, H. S., Park, K. S., & An, S. S., et al. (2015). Lamc2 enhances the metastatic potential of lung adenocarcinoma. Cell Death & Differentiation, 22(8), 1341-52.
Korbakis, D., Dimitromanolakis, A., Prassas, I., Davis, G. J., Barber, E., & Reckamp, K. L., et al. (2015). Serum lamc2 enhances the prognostic value of a multi-parametric panel in non-small cell lung cancer. British Journal of Cancer, 113(3), 484-491.
Kosanam, H., Prassas, I., Chrystoja, C. C., Soleas, I., Chan, A., & Dimitromanolakis, A., et al. (2013). Lamc2: a promising new pancreatic cancer biomarker identified by proteomic analysis of pancreatic adenocarcinoma tissues. Cell Death & Differentiation, 25(8), 1431-60.
Gong, J., Tian, J., Lou, J., Ke, J., Li, L., & Li, J., et al. (2016). A functional polymorphism in lnc-lamc2-1:1 confers risk of colorectal cancer by affecting mirna binding. Carcinogenesis, 37(5), 443-451.
Murgiano, L., Wiedemar, N., Jagannathan, V., Isling, L. K., Drögemüller, C., & Agerholm, J. S. (2015). Epidermolysa bullosa in danish hereford calves is caused by a deletion in lamc2 gene. BMC Veterinary Research,11,1(2015-02-07), 11(1), 23.

Quick Inquiry

Interested in learning more?

Contact us today for a free consultation with the scientific team and discover how Creative Biogene can be a valuable resource and partner for your organization.

Request a quote today!

Inquiry