Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene.

Kornblihtt, Alberto R.; Umezawa, Kazuo; Vibe-Pedersen, Karen; Baralle, Francisco E.

doi:10.1002/j.1460-2075.1985.tb03847.x

Cited by 633 publications

(311 citation statements)

References 32 publications

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“…Briefly, frozen sections were fixed with 4% (Kornblihtt et al, 1985) obtained from a papillary carcinoma was subcloned into pGEM plasmid (Promega, Madison, WI, USA). A 50-,ul aliquot of hybridization solution was placed on each section, and the sections were covered with siliconized coverglass and incubated at 50°C for 16 h in a moisture chamber.…”

Section: Methodsmentioning

confidence: 99%

Restricted expression of oncofetal fibronectin mRNA in thyroid papillary and anaplastic carcinoma: an in situ hybridization study

Takano

Matsuzuka²,

Miyauchi³

et al. 1998

Br J Cancer

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Restricted expression of oncofetal fibronectin mRNA in the tissues of thyroid papillary and anaplastic carcinoma has recently been shown by both Northern blot analysis and reverse transcriptase polymerase chain reaction (RT-PCR). Oncofetal fibronectin mRNA can be a target of gene diagnosis and targeted gene therapy, provided it is expressed in all cancer cells in the tissues. To investigate this criterion in thyroid cancer tissues, we measured their expression of oncofetal fibronectin mRNA using in situ hybridization. An abundant expression of oncofetal fibronectin mRNA was found in all the observed cancer cells of six papillary carcinomas and an anaplastic carcinoma, but not in the tissues of normal thyroid, Graves' disease, adenomatous goitre, follicular adenoma, follicular carcinoma or medullary carcinoma. This result encourages us to establish gene diagnosis of thyroid papillary and anaplastic carcinomas by detecting oncofetal fibronectin mRNA in biopsies. Images Figure 1

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Section: Methodsmentioning

confidence: 99%

Restricted expression of oncofetal fibronectin mRNA in thyroid papillary and anaplastic carcinoma: an in situ hybridization study

Takano

Matsuzuka²,

Miyauchi³

et al. 1998

Br J Cancer

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“…Domain 2 Fibronectin Type II Domain. The next region between amino acids 139 and 192 resembles the type II repeat of fibronectin with identity at 26 out of 62 amino acids (32). Although the precise function of this region is not known, it is likely that it may play a role in interaction with the extracellular matrix and may contribute to the spreading and adhesion of tissue macrophages that express the mannose receptor.…”

Section: Characteristics Of the Macrophage Mannose Receptormentioning

confidence: 99%

Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells.

Ezekowitz

Sastry

Bailly

et al. 1990

The Journal of Experimental Medicine

468

235

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SummaryThe macrophage mannose receptor is an integral membrane protein expressed on the surface of tissue macrophages . After ligation ofmannose-rich glycoconjugates or pathogens, the receptor mediates endorytosis and phagocytosis of the bound ligands by macrophages. The cDNAderived primary structure of the mannose receptor predicts a cysteine-rich NH2-terminal domain, followed by a fibronectin type II region. The remainder of the ectodomain is comprised of eight carbohydrate recognition-like domains, followed by a transmembrane region, and a cytoplasmic tail. Transfection of the mannose receptor cDNA into Cos-I cells is necessary for receptor-mediated endorytosis of mannose-rich glycoconjugate as well as phagocytosis of yeasts. Deletion of the cytoplasmic tail results in a mutant receptor that is able to bind but not ingest the ligated pathogens, suggesting that the signal for phagocytosis is contained in the cytoplasmic tail.P lasma clearance and cell uptake experiments (1) indicated the existence ofa receptor that bound glycoproteins bearing high mannose chains. Receptor activity was especially evident in the liver and spleens, although most other tissues were also positive. Subsequent experiments have established that the mannose receptor is expressed on the cell surface of tissue macrophages which reside in a wide anatomical distribution throughout most organs (2) . Although originally defined by its ability to mediate endorytosis ofmannosylated or fucosylated glycoproteins, the mannose receptor's predominant role appears to be in host defense. The receptor engages yeasts (3) and parasites (4) directly resulting in the engulfment of these particles and the release ofbiologically active secretory products like reactive oxygen intermediates (5), arachidonate metabolites (6), neutral proteinases (7), and monokines like IM and tumor necrosis factor (8) . As circulating monocytes do not express the mannose receptor on their cell surface (9), the functional role for the mannose receptor appears to be on tissue macrophages, which in addition to their localization in the reticular endothelial system line the alveolus and form a reticular network beneath epithelial surfaces in the skin, the gastrointestinal tract, kidney, and placenta (10). These sites are the portals of maximum antigen load and underscore the role for the mannose receptor in first line host defense.Recent experiments suggest that a circulating hepatocytederived serum mannose-binding protein is the functional serum equivalent of the tissue macrophage mannose receptor. The human mannose-binding protein (MBP)l is an acute-phase reactant (11) that binds certain viruses (12) and other mannose rich pathogens (13). Mannose-binding proteins after engaging organisms mediate attachment, uptake, and killing of opsonized bacteria by circulating phagocytes that do not express the mannose receptor (13). Underlying structural similarity between the MBP and the mannose receptor, thereby explaining their functional equivalence, was suggested by the discovery that h...

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“…Such domains with high similarity are usually called sequence motifs. Examples of such motifs are the fibronectin type 111 repeats (Kornblihtt et al, 1985) and the src homology domains 2 and 3 (Pawson & Gish, 1992). If it is possible to extract the essential information needed to define a motif, we can use this information to locate the motif in other sequences.…”

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confidence: 99%

Improving the sensitivity of the sequence profile method

1994

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The sequence profile method (Gribskov M, McLachlan AD, Eisenberg D, 1987, Proc Natl Acad Sci USA 844355-4358) is a powerful tool to detect distant relationships between amino acid sequences. A profile is a table of position-specific scores and gap penalties, providing a generalized description of a protein motif, which can be used for sequence alignments and database searches instead of an individual sequence. A sequence profile is derived from a multiple sequence alignment. We have found 2 ways to improve the sensitivity of sequence profiles: (1) Sequence weights: Usage of individual weights for each sequence avoids bias toward closely related sequences. These weights are automatically assigned based on the distance of the sequences using a published procedure (Sibbald PR, Argos P, 1990, JMolBiol216:813-818). (2) Amino acid substitution table: In addition to the alignment, the construction of a profile also needs an amino acid substitution

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Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene.

Cited by 633 publications

References 32 publications

Restricted expression of oncofetal fibronectin mRNA in thyroid papillary and anaplastic carcinoma: an in situ hybridization study

Restricted expression of oncofetal fibronectin mRNA in thyroid papillary and anaplastic carcinoma: an in situ hybridization study

Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells.

Improving the sensitivity of the sequence profile method

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