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Amyloid precursor protein is overexpressed in bladder cancer and contributes to the malignant bladder cancer cell behaviors.

08:00 EDT 18th July 2018 | BioPortfolio

Summary of "Amyloid precursor protein is overexpressed in bladder cancer and contributes to the malignant bladder cancer cell behaviors."

To investigate the expression of amyloid precursor protein in bladder cancer, and to study its role in malignant bladder cancer cell behaviors.

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This article was published in the following journal.

Name: International journal of urology : official journal of the Japanese Urological Association
ISSN: 1442-2042
Pages:

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Medical and Biotech [MESH] Definitions

Endopeptidases that are specific for AMYLOID PROTEIN PRECURSOR. Three secretase subtypes referred to as alpha, beta, and gamma have been identified based upon the region of amyloid protein precursor they cleave.

A precursor to the AMYLOID BETA-PROTEIN (beta/A4). Alterations in the expression of the amyloid beta-protein precursor (ABPP) gene, located on chromosome 21, plays a role in the development of the neuropathology common to both ALZHEIMER DISEASE and DOWN SYNDROME. ABPP is associated with the extensive extracellular matrix secreted by neuronal cells. Upon cleavage, this precursor produces three proteins of varying amino acid lengths: 695, 751, and 770. The beta/A4 (695 amino acids) or beta-amyloid protein is the principal component of the extracellular amyloid in senile plaques found in ALZHEIMER DISEASE; DOWN SYNDROME and, to a limited extent, in normal aging.

A disintegrin and metalloproteinase domain-containing protein. It cleaves the membrane-bound precursor of TUMOR NECROSIS FACTOR-ALPHA between ALANINE 76 and VALINE 77 to its functional form, as well as several other CELL SURFACE PROTEINS to their soluble forms, including AMYLOID BETA-PROTEIN PRECURSOR and PRION PROTEIN.

A type of extracellularly deposited substance composed of an amyloid protein and additional components including HEPARAN SULFATE PROTEOGLYCAN; LAMININ; COLLAGEN TYPE IV; SERUM AMYLOID P-COMPONENT; and APOLIPOPROTEINS E which together form characteristic amyloid fibrils. The core of amyloid fibrils is formed by the stacking of overlapping beta-pleated sheet domains of the amyloid protein. There are many different amyloid proteins that have been found forming the core of the fibrils in vivo. However, amyloid can be formed from any protein that exposes beta-pleated strand conformations during unfolding or refolding. A common characteristic of amyloid is the ability to bind such dyes as CONGO RED and thioflavine.

Proteins that form the core of amyloid fibrils. For example, the core of amyloid A is formed from amyloid A protein, also known as serum amyloid A protein or SAA protein.

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