Disease relevance of FNL1

• We propose that egg granuloma macrophages are activated in vivo to secrete a fibronectin-like molecule with activity that stimulates the directional migration of fibroblasts [1].
• Comparative adherence to human A549 cells, plant fibronectin-like protein, and polystyrene surfaces of four Pseudomonas fluorescens strains from different ecological origin [2].
• Secretion of a fibronectin-like substance from head and neck carcinomas [3].
• The secretion of a fibronectin-like substance in culture supernatants of cell lines of head and neck squamous cell carcinomas was observed [3].
• Sequence analysis of two human tenascin encoding cDNA clones from a cDNA library of the U251 glioblastoma cell line revealed the presence of a novel 276 bp tenascin type III fibronectin like repeat [4].

High impact information on FNL1

• A fibronectin-like protein was also isolated from the plasma of Torpedo fish [5].
• The nucleotide sequence and its deduced amino acid analysis revealed that this protein had immunoglobulin-like and fibronectin-like repeats [6].
• Serum levels of fibronectin and a fibronectin-like DNA-binding protein in patients with various diseases [7].
• Like titin, obscurin contains multiple immunoglobulin-like domains linked in tandem, but in contrast to titin it contains just two fibronectin-like domains [8].
• A strong, fibronectin-like attachment activity was present in (NH4)2SO4 precipitates of cell supernatant and sedimented with hexabrachions in glycerol gradients [9].

Biological context of FNL1

• These results clearly indicate that a sponge cell fibronectin-like protein may play an important role as the (or one of the) recognition site(s) of the aggregation factor(s) and can therefore be directly involved in cell association, morphogenesis, and differentiation [10].
• Fibronectin-like protein in Porifera: its role in cell aggregation [10].
• Alanine scanning mutagenesis and functional analysis of the fibronectin-like collagen-binding domain from human 92-kDa type IV collagenase [11].
• The cytoplasmic domain of integrin beta 4, which contains four type III fibronectin-like motifs, seems to be involved in the regulation of the assembly of hemidesmosomes (HD) and, therefore, in cell adhesion [12].
• Anti-adhesive glycosylation of fibronectin-like molecules in human placental matrix-type fibrinoid [13].

Anatomical context of FNL1

• This shows the predominant presence of a sponge fibronectin-like protein in the cell membranes and also its presence to a lesser extent in the intercellular matrix [10].
• The potential of the fibronectin-like collagen binding domain of 72-kDa gelatinase to bind extracellular matrix proteins may facilitate enzyme localization in connective tissue matrices [14].
• At ingression, quantitative adhesion assays demonstrated previously that primary mesenchyme cells (PMCs) change their affinity for neighboring cells, for a fibronectin-like substrate, and for the hyaline layer [15].
• Thus, during cultivation in vitro lymphocytes appear to synthesize a component with fibronectin-like properties [16].
• Fibronectin-like immunoreactivity in Helisoma buccal ganglia: evidence that an endogenous fibronectin-like molecule promotes neurite outgrowth [17].

Associations of FNL1 with chemical compounds

• One fibronectin-like repeat contains a single Arg-Gly-Asp sequence [18].
• The alpha 6 beta 4 integrin is structurally distinct from all the other known integrins because the cytoplasmic domain of beta 4 is unusually large and contains four type III fibronectin-like modules toward its C-terminus [19].
• The crude extract was further fractionated by DNA, heparin, and collagen affinity chromatography; they were termed Geodia fibronectin like fractions [20].
• Actin- and fibronectin-like proteins were characterized in the planarian, Dugesia lugubris s.l., by sodium dodecyl sulphate polyacrylamide gel electrophoresis and immunoblotting analysis using antisera to vertebrate actin and fibronectin [21].
• The clinical and milk isolates were the more efficient colonizers of polystyrene surfaces and also the more adherent to immobilized plant fibronectin-like protein [2].

Physical interactions of FNL1

• Most interestingly, we show that the anomalous lateral diffusion and, consequently, the binding to gelatin is greatly facilitated by the C-terminal hemopexin-like domain of the enzyme whereas the specificity of binding resides with the fibronectin-like gelatin-binding domain [22].

Regulatory relationships of FNL1

• This is the first direct biochemical demonstration of a fibronectin-like molecule in the sea urchin embryo which cross reacts with antibodies to vertebrate fibronectin [23].

Other interactions of FNL1

• The protein sequences deduced from Un1 and Un2 reveal an amino-terminal differentially spliced von Willebrand factor A domain, characteristic of proteins that interact with interstitial collagens, which is linked to fibronectin-like type III homology units by a unique sequence of 57 amino acids [24].
• Our results show a fibronectin-like molecule with an apparent molecular weight of 110 kDa in mature schizonts and microgametes [25].
• Seminal fibronectin-like antigen and transferrin concentrations in infertile and fertile men [26].
• The large TN-C isoform shows the same MMP-7-sensitive site adjacent to the NH2-terminal sequence, but is further degraded in the splicing area where three fibronectin-like type III repeats are completely digested [27].
• Here, human N2-B-cardiac PEVK was expressed in Escherichia coli and tested-along with recombinant cardiac titin constructs containing immunoglobulin-like or fibronectin-like domains-for a possible interaction with actin filaments [28].

Analytical, diagnostic and therapeutic context of FNL1

• In addition, the immunohistochemical distribution of both actin- and fibronectin-like material was examined by using immuno-electron microscopy [21].
• Western blots using both antibodies revealed that the PLF-CM contained laminin- and fibronectin-like molecules [29].

References