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- Table of Contents
Facts about Kallikrein-14.
May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a procedure by which the most superficial corneocytes are shed from the skin surface.
Human | |
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Gene Name: | KLK14 |
Uniprot: | Q9P0G3 |
Entrez: | 43847 |
Belongs to: |
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peptidase S1 family |
EC 3.4.21; EC 3.4.21.-; hK14; Kallikrein 14; Kallikrein-like protein 6; kallikrein-related peptidase 14; KLK14; KLKL6; KLK-L6kallikrein-14
Mass (kDA):
29.122 kDA
Human | |
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Location: | 19q13.41 |
Sequence: | 19; NC_000019.10 (51077494..51084210, complement) |
Highly expressed in CNS, bone marrow and fetal liver. Also expressed in breast, thyroid, kidney, colon, pancreas, spleen, prostate, uterus, small intestine, placenta and skeletal muscle. Among 40 tissues tested, the highest expression is detected in skin followed by breast and prostate (at protein level). Expressed in stratum corneum by sweat ducts and sweat glands and detected in sweat (at protein level).
Secreted, extracellular space.
There are many ways you can use the KLK14 marker, including studies that examine its high binding ability, interactions with HAI-1 or HAI-2 serine protease inhibitors, as well as combinations with other markers. Boster Bio has more information about this protein. This article explores the best uses of KLK14. For more information about the protein's effects upon tumor growth, see this article.
Kallikrein 14, an serine protease has been associated to many human pathologies. Its function remains a mystery, but it has been proven to positively correlate the Gleason score. KLK14, a protein that proteolytically inhibits HGF activator/inhibitor 1, (HAI-1), is an example of a protein. Homology modeling was used to determine the affinities of KLK14 with HAI-1. The free energies of the interaction between these two proteins were higher that previously thought.
The present invention is best used with biological samples that are modulated using hormone levels. These samples can be from a patient with a disease or a healthy person who has a precursor to the disease. In some cases, these samples can be used to diagnose patients with disease. These findings are still in early stages of development and can be used to create personalized medicines for patients.
Steven Boster started developing the ELISA in 1990. After generating hundreds of primary antibody, Boster was known as "he who converted science in the lavatory". Boster Bio became China's largest catalog antibody manufacturer by the late nineties. PicoKine(tm), a proprietary ELISA platform developed by Boster Bio, provides high-sensitivity ELISA kits to research.
Recent studies have shown that the KLK14 marker's high binding affinity in ELISAs allows for the detection of human keratinocytes across a wide variety of tissues and cell types. KLK5 is a major serine protease expressed in epidermis and secreted by cytoplasmic microorgans in the stratum granulosum. This protein is thought that it acts in an acidic environment within the extracellular space. It may also have other functions when there are neutral pH conditions.
A proximity ligation test confirmed the high binding ability of the KLK14 marker from the Boster Bio ELISA. Antibodies against the KLK5 and profilaggrin C terminus were used as positive controls. The results showed that the proteins interact within a radius 40 nm. The binding affinities of KLK14 markers were also observed in cell membranes, and granular tissues.
The KLK14 marker showed a different binding affinity in ELISAs due to the stability within the hydrogen-bond networks between the arginine atom and the KLK14 S1 pocket. Asp174 and Trp196 are hotspots for binding in KLK14. Further research is required to determine the molecular foundation of these findings.
AEBSF is a potent inhibitor of organic kallikrein. It significantly inhibited the rhKLK5-induced cleavage wild-type filaggrin fusion proteins at a concentration one milligram. This strongly suggests that KLK5 may be targeting the filaggrin linker domain in order to process the protein. The Boster bio KLK5 marker is the best option for studies involving this particular protein.
The co-expression matriptase was performed with normal epithelial cell lines in the first phase. The cells were analysed using magnetic resonance imaging. The results showed that in vitro and vivo growth of gastric tumor cells was inhibited by matriptase. Furthermore, the inhibitors inhibited apoptosis in tumors in a phase II trial.
The HAI-1 inhibitors domain showed significant inhibitions in hepsin, matriptase and HGFA. These findings suggest that HAIs may have a therapeutic potential in urological cancers. Further research will be required to determine the exact mechanism of HAI-1 as well as HAI-2 inhibition.
HAI-2 not only inhibits the activating proteases; it also serves a dual role. It activates caspase-3 which is a cell-selective, apoptotic factor in esophageal carcinoma squamous cell. Invasive growth can also be prevented by inhibiting caspase-3. These findings suggest HAI-2 might be tissue-specific.
HAI-1 and HAI-2 seline protease inhibitors have a positive impact on matriptase activity. HAI-2 seline protease inhibitors block matriptase transport to the cell's surface and activate the matriptase. This leads to an increase in HGF activity in bone metastasis.
Fischer's study sheds some light on the interaction between HAI-1 inhibitors and HAI-2 inhibitors. Inhibitors play a critical role when certain cancers develop. HAI-1 inhibitors and HAI-2 inhibitors interact to inhibit both of these processes. The results also indicate that the two inhibitors have opposite effects on the immune system.
Matriptase is a type II transmembrane serine protease that is expressed in most human epithelia. HAI-1 interacts via sequential N terminal cleavage and transient association with HAI-1. HAI-1 can be overexpressed and prevents matriptase induced skin tumors.
This interaction is catalytically efficient. The enzyme's pK(a), which is the enzyme's active site, is increased by the hydroxyanion stabilization. The hydroxyl group in serine is also decreased by the inhibitors. This is why the high catalytic efficacy. This interaction has important implications on drug development. HAI-1 & HAI-2 serine proteases also inhibit the synthesis and use of acetaminophen, a cytotoxic substance.
Different tests can show different patterns of cancer cells, and they often work well together. Combinations of three or four markers improve the sensitivity of tests and increase specificity. These combinations can have decreased sensitivities and specificities, however. The combination FISH and uCyt+ testing have the highest sensitivity as well as specificity. The same applies to cytology and uCyt+. False positive results can also result from a single positive marker.
Combining total PSA (and free-form PSA) can increase cancer-specificity. Other combinations include AFP/CA19-9. Other markers commonly used in combination include CYFRA21-1. It indicates the presence of neuroendocrine carcinomas. The ratio PG I/PG 2 indicates the condition of the gastric mucosa. These tests can however be expensive. To detect the disease, it is best to use three to four markers.
PMID: 11309303 by Yousef G.M., et al. Cloning of a new member of the human kallikrein gene family, KLK14, which is down-regulated in different malignancies.
PMID: 11352573 by Hooper J.D., et al. Identification and characterization of KLK14, a novel kallikrein serine protease gene located on human chromosome 19q13.4 and expressed in prostate and skeletal muscle.