Last update 01 Nov 2024

cysteine protease x CD10

Last update 01 Nov 2024

Basic Info

Related Targets

cysteine proteaseCD10

Drugs associated with cysteine protease x CD10

ALV-002

Target

CD10 x cysteine protease

Mechanism

cysteine protease stimulants [+1]

Active Org.-

Originator Org.

Alvine Pharmaceuticals, Inc.

Active Indication-

Inactive Indication

Intestinal Diseases

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with cysteine protease x CD10

100 Translational Medicine associated with cysteine protease x CD10

0 Patents (Medical) associated with cysteine protease x CD10

Literatures (Medical) associated with cysteine protease x CD10

01 May 2014·American Journal of Surgical PathologyQ1 · MEDICINE

Expanded Immunohistochemical Profile Emphasizing Novel RCC Markers and Report of 10 New Genetically Confirmed Cases

Q1 · MEDICINE

Article

Author: Kerry Morris ; Mohamed Allaf ; George J. Netto ; Mahul B. Amin ; Pedram Argani ; Jonathan I. Epstein ; Victor E. Reuter ; Nathaniel E. Smith ; Peter B. Illei ; Jessica Hicks ; Angelo DeMarzo ; Nilda Gonzalez

Renal cell carcinomas (RCCs) harboring the t(6;11)(p21;q12) translocation were first described in 2001 and recently recognized by the 2013 International Society of Urological Pathology Vancouver Classification of Renal Neoplasia. Although these RCCs are known to label for melanocytic markers HMB45 and Melan A and the cysteine protease cathepsin K by immunohistochemistry (IHC), a comprehensive IHC profile has not been reported. We report 10 new t(6;11) RCCs, all confirmed by break-apart TFEB fluorescence in situ hybridization. A tissue microarray containing 6 of these cases and 7 other previously reported t(6;11) RCCs was constructed and immunolabeled for 21 different antigens. Additional whole sections of t(6;11) RCC were labeled with selected IHC markers. t(6;11) RCC labeled diffusely and consistently for cathepsin K and Melan A (13 of 13 cases) and almost always at least focally for HMB45 (12 of 13 cases). They labeled frequently for PAX8 (14 of 23 cases), CD117 (10 of 14 cases), and vimentin (9 of 13 cases). A majority of cases labeled at least focally for cytokeratin Cam5.2 (8 of 13 cases) and CD10 and RCC marker antigen (10 of 14 cases each). In contrast to a prior study's findings, only a minority of cases labeled for Ksp-cadherin (3 of 19 cases). The median H score (product of intensity score and percentage labeling) for phosphorylated S6, a marker of mTOR pathway activation, was 101, which is high relative to most other RCC subtypes. In summary, IHC labeling for PAX8, Cam5.2, CD10, and RCC marker antigen supports classification of the t(6;11) RCC as carcinomas despite frequent negativity for broad-spectrum cytokeratins and EMA. Labeling for PAX8 distinguishes the t(6;11) RCC from epithelioid angiomyolipoma, which otherwise shares a similar immunoprofile. CD117 labeling is more frequent in the t(6;11) RCC compared with the related Xp11 translocation RCC. Increased pS6 expression suggests a possible molecular target for the uncommon t(6;11) RCCs that metastasize.

01 Jun 2011·Neurobiology of DiseaseQ2 · MEDICINE

Mechanism mediating oligomeric Aβ clearance by naïve primary microglia

Q2 · MEDICINE

Article

Author: Fong Lee Huang ; Bo Shen Guo ; Cheng Ning Yang ; Huey Jen Tsay ; Pei Hao Chen ; Young Ji Shiao ; Yi Jen Chen ; Chi Yuan Cho ; Feng Shiun Shie

The accumulation of soluble oligomeric amyloid-β peptide (oAβ) proceeds the formation of senile plaques and contributes to synaptic and memory deficits in Alzheimer's disease (AD). The mechanism of mediating microglial oAβ clearance remains unclear and thought to occur via scavenger receptors (SRs) in microglia. SRs respond to their ligands in a subtype-specific manner. Therefore, we sought to identify the specific subtypes of SRs that mediate oAβ internalization and proteases that degrade oAβ species in naïve primary microglia. The component of oAβ species were characterized by western blot analysis, analytical ultracentrifugation analysis, and atomic force microscopy. The oAβ species remained soluble in the medium and microglial lysates during incubation at 37 °C. SR-A, but not CD36, mediated oAβ internalization in microglia as suggested by the use of subtype-specific neutralizing antibodies and small interfering RNAs (siRNAs). Immunoprecipitation analysis showed that oAβ interacted with SR-A on the plasma membrane. After internalization, over 40% of oAβ vesicles were trafficked toward lysosomes and degraded by cysteine proteases, including cathepsin B. The inhibitors of proteasome, neprilysin, matrix metalloproteinases, and insulin degrading enzyme failed to protect internalized oAβ from degradation. Our study suggests that SR-A and lysosomal cathepsin B are critical in microglial oAβ clearance, providing insight into how microglia are involved in the clearance of oAβ and their roles in the early stages of AD.

01 Jan 2003·Scandinavian Journal of ImmunologyQ4 · MEDICINE

Downregulation of Mac‐1 Expression in Monocytes by Surface‐Bound IgG

Q4 · MEDICINE

Article

Author: J. Geffner ; M. Vermeulen ; A. Trevani ; G. Salamone ; R. Gamberale ; P. X. Fernández‐Calotti ; M. Giordano

AbstractPhysical and functional association between the β2‐integrin Mac‐1 (CD11b/CD18) and receptors of immunoglobulin G (IgG) (FcγRs) has been previously reported. In this study, we examined the modulation of Mac‐1 expression by IgG in different leucocyte populations. Our data show that human monocytes, but not neutrophils, macrophages, dendritic or natural killer cells, downregulate the expression of Mac‐1 after overnight exposure to surface‐bound IgG. This effect, which requires at least 6 h of incubation, is not associated with a general downmodulation of membrane antigens, and is selectively induced by immobilized IgG (iIgG), as the stimulation of monocytes with N‐formyl‐methionyl‐leucyl‐phenylalanine, lipopolysaccharide, tumour necrosis factor‐α (TNF‐α) or soluble IgG did not modify the Mac‐1 expression after 18 h in culture. The loss of Mac‐1 was completely prevented by blocking antibodies (Abs) directed to FcγRII (CD32) or CD18. On the other hand, the serine protease inhibitor, phenyl methyl sulphonyl fluoride, but not inhibitors of cysteine proteases or neutral endopeptidases, partially prevented the downregulation of Mac‐1 by iIgG. Monocytes cultured overnight on iIgG exhibited a dramatic decrease in their capacity to ingest zymosan particles that could be attributed to the reduced expression of Mac‐1. However, there was no inhibition of TNF‐α production induced by zymosan, suggesting that Mac‐1‐dependent responses require different levels of its expression to be fully activated.

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