Dipeptidyl Peptidase-4-Mediated Fibronectin Processing Evokes a Profibrotic Extracellular Matrix.

Fibronectin serves as a platform to guide and facilitate deposition of collagen and fibrillin microfibrils. During development of fibrotic diseases, altered fibronectin deposition in the extracellular matrix (ECM) is generally an early event. After this, dysregulated organization of fibrillins and fibrillar collagens occurs.

Diversity of amyloid beta peptide actions.

Fibril formation by amyloidogenic proteins and peptides is considered the cause of a number of incurable diseases. One of the most known amyloid diseases is Alzheimer's disease (AD). Traditionally, amyloidogenic beta peptides Aβ40 and Aβ42 (Aβs) are considered as main causes of AD and the foremost targets in AD fight.

Citrullination of adenosine deaminase impairs its binding to dipeptidyl peptidase IV.

The presence of citrullinated adenosine deaminase (ADA) was reported in the synovial fluids of rheumatoid arthritis individuals. This work reports the effects of ADA citrullination on the formation/stabilization of ADA complex with dipeptidyl peptidase IV (DPPIV). The electrophoretic mobility of in vivo citrullinated ADA was diminished compared to the native one.

Adenosine deaminase - A target for new piperazine derivatives.

The level of adenosine deaminase (ADA) activity increases in pathological effusions. Therefore, the concentration of its substrate, anti-inflammatory adenosine, decreases, thereby aggravating inflammation. Hence, the quest for ADA inhibiting compounds is an actual problem in medicine and pharmacology.

Concerted action of dipeptidyl peptidase IV and glutaminyl cyclase results in formation of pyroglutamate-modified amyloid peptides in vitro.

Compelling evidence suggests a crucial role of amyloid beta peptides (Aβ(1-40/42)) in the etiology of Alzheimer's disease (AD). The N-terminal truncation of Aβ(1-40/42) and their modification, e.g.

Activity of enzymes of adenyline compounds metabolism during crush and decompression of muscle tissue. Part II. Adenosine deaminase activity at experimental crush syndrome.

Introduction: Publications on investigation of crush syndrome pathogenesis, particularly of enzymatic systems upon traumatic toxicosis are rather limited. Such investigations are necessary for opportune diagnosis and definition of a treatment tactic. To replenish this deficiency, the adenosine deaminase level was studied in 12 rat tissues at experimental crush syndrome in vivo.