|
SNED1
SNED1 (Sushi, Nidogen, and EGF-like Domains) is an extracellular matrix (ECM) protein expressed at low levels in a wide range of tissues. The gene encodinSNED1is located in the human chromosome 2 at locus q37.3. The corresponding mRNA isolated from the spleen and is 6834bp in length, and the corresponding protein i1413 amino-acid long The mouse ortholog of SNED1 was cloned in 2004 from the embryonic kidney by Leimester et al. SNED1 present domains characteristic of ECM proteins, including an amino-terminal NIDO domain, several calcium binding EGF-like domains (EGF_CA), a Sushi domain also known as complement control protein (CCP) domain, and three type III fibronectin (Fibronectin type III domain, FN3) domains in the carboxy-terminal region. Gene Locus SNED1 is located on the plus strand of chromosome 2 at locus 2q37.3. The Refseq identification number iNM_001080437.3The genomic DNA sequence of SNED1 contains 98,159bp and the longest spliced mRNA as predicted by AceView is 70 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibronectin Type III Domain
The Fibronectin type III domain is an evolutionarily conserved protein domain that is widely found in animal proteins. The fibronectin protein in which this domain was first identified contains 16 copies of this domain. The domain is about 100 amino acids long and possesses a beta sandwich structure. Of the three fibronectin-type domains, type III is the only one without disulfide bonding present. Fibronectin domains are found in a wide variety of extracellular proteins. They are widely distributed in animal species, but also found sporadically in yeast, plant and bacterial proteins. Human proteins containing this domain ABI3BP; ANKFN1; ASTN2; AXL; BOC; BZRAP1; C20orf75; CDON; CHL1; CMYA5; CNTFR; CNTN1; CNTN2; CNTN3; CNTN4; CNTN5; CNTN6; COL12A1; COL14A1; COL20A1; COL7A1; CRLF1; CRLF3; CSF2RB; CSF3R; DCC; DSCAM; DSCAML1; EBI3; EGFLAM; EPHA1; EPHA10; EPHA ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sushi Domain
Sushi domain is an evolutionarily conserved protein domain. It is also known as Complement control protein (CCP) modules or short consensus repeats (SCR). The name derives from the visual similarity of the domain to nigiri sushi when the primary structure is drawn showing the loops created by the disulfide bonds. Sushi domains exist in a wide variety of complement and adhesion proteins. The structure is known for this domain; it is based on a beta-sandwich arrangement - one face made up of three β-strands hydrogen-bonded to form a triple-stranded region at its centre, and the other face formed from two separate β-strands. CD21 (also called C3d receptor, CR2, Epstein Barr virus receptor or EBV-R) is the receptor for EBV and for C3d, C3dg and iC3b. Complement components may activate B cells through CD21. CD21 is part of a large signal-transduction complex that also involves CD19, CD81, and Leu13. Some of the proteins in this group are responsible for the molecular basis of t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EGF-like Domain
The EGF-like domain is an evolutionary conserved protein domain, which derives its name from the epidermal growth factor where it was first described. It comprises about 30 to 40 amino-acid residues and has been found in a large number of mostly animal proteins. Most occurrences of the EGF-like domain are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted. An exception to this is the prostaglandin-endoperoxide synthase. The EGF-like domain includes 6 cysteine residues which in the epidermal growth factor have been shown to form 3 disulfide bonds. The structures of 4-disulfide EGF-domains have been solved from the laminin and integrin proteins. The main structure of EGF-like domains is a two-stranded β-sheet followed by a loop to a short C-terminal, two-stranded β-sheet. These two β-sheets are usually denoted as the major (N-terminal) and minor (C-terminal) sheets. EGF-like domains frequently occur in numerous tandem copies in pro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Extracellular Matrix
In biology, the extracellular matrix (ECM), also called intercellular matrix, is a three-dimensional network consisting of extracellular macromolecules and minerals, such as collagen, enzymes, glycoproteins and hydroxyapatite that provide structural and biochemical support to surrounding cells. Because multicellularity evolved independently in different multicellular lineages, the composition of ECM varies between multicellular structures; however, cell adhesion, cell-to-cell communication and differentiation are common functions of the ECM. The animal extracellular matrix includes the interstitial matrix and the basement membrane. Interstitial matrix is present between various animal cells (i.e., in the intercellular spaces). Gels of polysaccharides and fibrous proteins fill the Interstitial fluid, interstitial space and act as a compression buffer against the stress placed on the ECM. Basement membranes are sheet-like depositions of ECM on which various epithelial cells rest ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibrolytic
Fibrolytic bacteria constitute a group of microorganisms that are able to process complex plant polysaccharides thanks to their capacity to synthesize cellulolytic and hemicellulolytic enzymes. Polysaccharides are present in plant cellular cell walls in a compact fiber form where they are mainly composed of cellulose and hemicellulose. Fibrolytic enzymes, which are classified as cellulases, can hydrolyze the β (1 ->4) bonds in plant polysaccharides. Cellulase and hemicellulase (also known as xylanase) are the two main representatives of these enzymes. Biological characteristics Fibrolytic bacteria use glycolysis and the pentose phosphate pathway as the main metabolic routes to catabolize carbohydrates in order to obtain energy and Carbon, carbon backbones. They use ammonia as the major and practically exclusive source of nitrogen, and they require several B-vitamins for their development. They often depend on other microorganisms to obtain some of their nutrients. Although their ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transcription Factor
In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription of genetic information from DNA to messenger RNA, by binding to a specific DNA sequence. The function of TFs is to regulate—turn on and off—genes in order to make sure that they are expressed in the desired cells at the right time and in the right amount throughout the life of the cell and the organism. Groups of TFs function in a coordinated fashion to direct cell division, cell growth, and cell death throughout life; cell migration and organization (body plan) during embryonic development; and intermittently in response to signals from outside the cell, such as a hormone. There are up to 1600 TFs in the human genome. Transcription factors are members of the proteome as well as regulome. TFs work alone or with other proteins in a complex, by promoting (as an activator), or blocking (as a repressor) the recruitment of RNA ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Spermine Synthase
Spermine synthase (, ''spermidine aminopropyltransferase'', ''spermine synthetase'') is an enzyme that converts spermidine into spermine. This enzyme catalyses the following chemical reaction : S-adenosylmethioninamine + spermidine \rightleftharpoons S-methyl-5'-thioadenosine + spermine Spermine synthase is an enzyme involved in polyamine biosynthesis. It is present in all eukaryotes and plays a role in a variety of biological functions in plants Its structure consists of two identical monomers of 41 kDa with three domains each, creating a homodimer formed via dimerization A dimer () (''wikt:di-, di-'', "two" + ''-mer'', "parts") is an oligomer consisting of two monomers joined by bonds that can be either strong or weak, Covalent bond, covalent or Intermolecular force, intermolecular. Dimers also have significant im .... The interactions between one of the three domains, the N-terminals of the monomers, is responsible for dimerization as that is where the active site is located; ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Somatostatin Receptor 2
Somatostatin receptor type 2 is a protein that in humans is encoded by the ''SSTR2'' gene. The SSTR2 gene is located on chromosome 17 on the long arm in position 25.1 in humans. It is also found in most other vertebrates. The somatostatin receptor 2 (SSTR2), which belongs to the G-protein coupled receptor family, is a protein which is most highly expressed in the pancreas (both alpha- and beta-cells), but also in other tissues such as the cerebrum and kidney and in lower amount in the jejunum, colon and liver. In the pancreas, after binding to somatostatin, it inhibits the secretion of pancreatic enzymes. During development, it stimulates neuronal migration and axon outgrowth. The somatostatin receptor 2 is expressed in most tumors. Patients with neuroendocrine tumors that over-express the somatostatin receptor 2 have an improved prognosis. The over expression of SSTR2 in tumors can be exploited to selectively deliver radio-peptides to tumors to either detect or destroy them. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Somatostatin
Somatostatin, also known as growth hormone-inhibiting hormone (GHIH) or by several other names, is a peptide hormone that regulates the endocrine system and affects neurotransmission and cell proliferation via interaction with G protein-coupled somatostatin receptors and inhibition of the release of numerous secondary hormones. Somatostatin inhibits insulin and glucagon secretion. Somatostatin has two active forms produced by the alternative cleavage of a single preproprotein: one consisting of 14 amino acids (shown in infobox to right), the other consisting of 28 amino acids. Among the vertebrates, there exist six different somatostatin genes that have been named ''SS1, SS2, SS3, SS4, SS5'' and ''SS6''. Zebrafish have all six. The six different genes, along with the five different somatostatin receptors, allow somatostatin to possess a large range of functions. Humans have only one somatostatin gene, ''SST''. Nomenclature Synonyms of "somatostatin" include: * growth hormoneâ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Basement Membrane
The basement membrane is a thin, pliable sheet-like type of extracellular matrix that provides cell and tissue support and acts as a platform for complex signalling. The basement membrane sits between Epithelium, epithelial tissues including mesothelium and endothelium, and the underlying connective tissue. Structure As seen with the electron microscope, the basement membrane is composed of two layers, the basal lamina and the reticular lamina. The underlying connective tissue attaches to the basal lamina with collagen VII anchoring fibrils and fibrillin microfibrils. The basal lamina layer can further be subdivided into two layers based on their visual appearance in electron microscopy. The lighter-colored layer closer to the epithelium is called the lamina lucida, while the denser-colored layer closer to the connective tissue is called the lamina densa. The Electron microscope, electron-dense lamina densa layer is about 30–70 nanometers thick and consists of an underlying ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Collagen
Collagen () is the main structural protein in the extracellular matrix found in the body's various connective tissues. As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen consists of amino acids bound together to form a triple helix of elongated fibril known as a collagen helix. It is mostly found in connective tissue such as cartilage, bones, tendons, ligaments, and skin. Depending upon the degree of mineralization, collagen tissues may be rigid (bone) or compliant (tendon) or have a gradient from rigid to compliant (cartilage). Collagen is also abundant in corneas, blood vessels, the gut, intervertebral discs, and the dentin in teeth. In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue and accounts for 6% of the weight of the skeletal muscle tissue. The fibroblast is the most common cell that crea ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
.svg "Click for more on -> Collagen")