Disease relevance of LAMA1

• Keratosis pilaris/ulerythema ophryogenes and 18p deletion: is it possible that the LAMA1 gene is involved [1]?
• cDNA clones for the human laminin A chain were isolated from libraries prepared from human gestational choriocarcinoma cell line (JAR) RNA [2].
• A 19 amino acid synthetic peptide derived from the E8 fragment of the laminin A chain (Cys-Ser-Arg-Ala-Arg-Lys-Gln-Ala-Ala-Ser-Ile-Lys-Val-Ala-Val-Ser-Ala-Asp -Arg- NH2) was identified which promotes metastasis and stimulates collagenase IV activity in the culture medium of B16 melanoma cells (Kanemoto et al., 1990) [3].
• Isolation of shiga toxin-producing Escherichia coli from a South American camelid (Lama guanicoe) with diarrhea [4].
• A syndrome characterized by anemia, erythrocyte dyscrasia, low body weight, and hypothyroidism was observed in 8 llamas (Lama glama) [5].

High impact information on LAMA1

• Neuroscience meeting draws fire over Dalai Lama lecture [6].
• This specific cell killing was not T-cell receptor mediated, but it was inhibited by addition of the anti-monomeric laminin receptor MAb MLuC5 and by a synthetic peptide corresponding to amino acids 2091-2108 of the laminin A chain [7].
• Reciprocal expression of laminin A-chain isoforms along the crypt-villus axis in the human small intestine [8].
• A synthetic peptide derived from the carboxy terminus of the laminin A chain represents a binding site for the alpha 3 beta 1 integrin [9].
• Using synthetic peptides, we have identified an amino acid sequence within the carboxy-terminal region of the laminin A chain that is recognized by the alpha 3 beta 1 integrin [9].

Chemical compound and disease context of LAMA1

• For each of 3 separate evaluations, 6 fasted llamas (Lama glama) were sedated with xylazine (1.1 mg/kg of body weight, IV) and then 15 minutes later were given normal saline solution (5.0 ml, IV; control values), doxapram (2.2 mg/kg, IV), or 4-amino-pyridine (0.3 mg/kg, IV) and yohimbine (0.125 mg/kg, IV) [10].

Biological context of LAMA1

• LAMA1 and LAMA3 genes are located on chromosome 18 [11].
• Amino acid sequence analysis demonstrated that the 5-kDa fragment originates with the fibronectin amino terminus whereas the laminin fragment was derived from the carboxyl-terminal globular domain of the laminin A chain [12].
• Lysine binding site-dependent binding of soluble laminin to immobilized plasminogen kringles 1-5 as well as an additional lysine binding site-independent interaction between mini-plasminogen and the 38-kDa laminin A chain fragment were also observed [12].
• A human placental lambdagt11 expression cDNA library was probed for laminin cDNAs by a combination of immunoscreening using polyclonal anti-human laminin antibody, and plaque hybridizations using a mouse laminin A chain cDNA [13].
• The effect of substituted laminin A chain-derived peptides on the conformation and activation kinetics of plasminogen [14].

Anatomical context of LAMA1

• Appearance and distribution of laminin A chain isoforms and integrin alpha 2, alpha 3, alpha 6, beta 1, and beta 4 subunits in the developing human small intestinal mucosa [15].
• We demonstrate that the Lama construct can direct the expression of a heterologous cDNA encoding the C-terminal peptide of human factor VIII to salivary glands and that the corresponding peptide is secreted into saliva [16].
• Basal lamina formation by epithelial cell lines correlates with laminin A chain synthesis and secretion [17].
• Synthetic peptides from the cross-region of the laminin A chain were prepared and tested for their biological activities, especially for neurite outgrowth [18].
• Interaction of endothelial cells with a laminin A chain peptide (SIKVAV) in vitro and induction of angiogenic behavior in vivo [19].

Associations of LAMA1 with chemical compounds

• Sulfatide-binding domain of the laminin A chain [20].
• Interactions between the proteasome inhibitor bortezomib and histone deacetylase inhibitors (HDIs) have been examined in Bcr/Abl+ human leukemia cells (K562 and LAMA 84) [21].
• Similar events were observed in other Bcr/Abl(+) cells (i.e., LAMA 84), and in cells exposed to STI571 in combination with the HDI sodium butyrate [22].
• The sequence similarity corresponds to the G domain of laminin A chain, which binds heparin and type IV collagen [23].
• STI571 and SAHA also interacted synergistically to induce apoptosis in STI571-resistant K562 and LAMA 84 cells that display increased Bcr/Abl protein expression [22].

Physical interactions of LAMA1

• Amino acid sequencing of the approximately 55 kDa fragment identified a conformationally dependent Abeta-binding site within laminin localized to the globular repeats on the laminin A chain [24].

Enzymatic interactions of LAMA1

• We have previously demonstrated that a synthetic peptide derived from amino acids 2091-2108 of the laminin A chain (designated LamA2091-2108) can significantly enhance t-PA-catalyzed Pg activation [14].

Other interactions of LAMA1

• The genes for these chains are LAMA1, LAMB1 and LAMC1, respectively [25].
• Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a partial cDNA encoding a variant laminin A chain [26].
• Products from the proteolytic cleavage of the A and B2 chains of laminin were observed with the sites of cleavage determined to be at position 2666 in the laminin A chain and position 1238 in the laminin B2 chain [27].
• Next is domain III which shares homology to the short arm of laminin A chain and contains four cysteine-rich regions intercalated among three globular domains [28].
• Activated MMP-9 digested gelatin, type-V collagen, reduced carboxymethylated transferrin and, to a lesser extent, type-IV collagen and laminin A chain [29].

Analytical, diagnostic and therapeutic context of LAMA1

• Following proteolytic digestion with thermolysin, an intact fragment of the laminin A chain carboxyl-terminal domain exhibiting sulfatide-binding activity was isolated using gel filtration and heparin affinity chromatography [20].
• Northern-blot analysis was used to study the laminin A chain expression in the JAR cell line, full-term placenta and newborn-human tissues (kidney, spleen, lung, heart muscle, psoas muscle and diaphragm muscle) [2].
• These cDNAs were utilized for chromosomal in situ hybridizations to establish the genomic location of the laminin A chain gene [30].
• Electron microscopy and cDNA sequencing show a complex and elongated domain structure for the core protein which in part is homologous to that of the laminin A chain [31].
• Molecular cloning of the cDNA encoding human laminin A chain [32].

References