Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:4.1.2.13 (
aldolase
)
3,461
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Tarsal
degenerative joint disease
(
DJD
) in 27 cattle was classified as primary or secondary based on age, joint conformation defects, faulty hindlimb alignment, or history of trauma to the affected joint(s). Results of blood and synovial fluid analysis for cattle affected with primary or secondary tarsal
DJD
were grouped in compilation of data. Cattle with tarsal
DJD
had significantly (P smaller than 0.01) reduced hemoglobin (Hb) content in comparison to that in control cattle. There was highly significant (P smaller than 0.001) reduction in packed cell volume (PCV). A significant difference was not determined for mean corpuscular hemoglobin concentration (MCHC) values of the 2 groups of cattle. Total white blood cell (WBC) counts closely paralleled each other, although mean proportion of neutrophils was significantly (P smaller than 0.05) greater in cattle affected with tarsal
DJD
, as were mean proportion of lymphocytes (P smaller than 0.02). Synovial fluid samples were analyzed for physical, biochemical, and cytologic properties. Statistical comparisons were made between values determined for arthritic cattle and control cattle. All samples from cattle with tarsal
DJD
were transudative. Opacity and flocculation were attributed to the presence of cartilaginous fragments and fibrils. There was significant correlation between increased relative viscosity (RV) and higher grades of mucinous precipitate quality (MPQ; r = +0.294, P smaller than 0.05) for all cattle. Mean alkaline phosphatase (ALP) activity for arthritic cattle was significantly (P smaller than 0.001) reduced, as was the mean activity for lactic dehydrogenase (LDH; P smaller than 0.05). The mean
aldolase
(
ALD
) activity for arthritic cattle was increased, whereas mean activity values for glutamic oxalacetic transaminase (GOT) and glutamic pyruvic transaminase (GPT) were reduced. Samples from arthritic cattle had reduced total leukocyte counts and significantly (P smaller than 0.05) increased proportion of macrophages in comparison to the values in control cattle.
...
PMID:Tarsal degenerative joint disease in cattle: blood and synovial fluid changes. 114 40
Osteoarthritis
(OA) is characterized by cartilage degradation. The chondrocyte is the only cell type present in mature cartilage, and it is important in the control of cartilage integrity. The aim of this study was to analyze, by a proteomic approach, the changes that are characteristic of OA chondrocytes, and to identify new OA-related proteins. Chondrocytes were isolated from the cartilage of ten OA patients undergoing joint replacement and ten donors with no history of joint disease. Whole-cell proteins were resolved by 2-DE and stained with SYPRO Ruby. Protein expression patterns of 2-DE gels from OA and normal chondrocyte proteins were analyzed with PDQuest 7.3.1 software. OA-related proteins were identified by MALDI-TOF or MALDI-TOF/TOF MS. The results were validated for ANXA1, GSTO1, GRP78, and HSP90beta in cells by Western blotting and in tissue cartilage by immunohistochemistry. Results showed an average of 700 protein spots that were present in the 2-DE gels. Compared to normal chondrocytes, 19 protein spots were found to be significantly increased in OA cells (ratio OA:N> or =2.0, p<0.05), whereas nine were decreased in OA chondrocytes (ratio OA:N< or =0.5, p<0.05). Three stress response proteins were increased (HSP90beta, GRP78, and GRP94) and three proteins involved in glycolysis were decreased (enolase, glyceraldehyde 3-phosphate dehydrogenase, and fructose biphosphate
aldolase
). Functionally, almost all proteins could be classified as proteins involved in cellular metabolism (33%), structure (21%), or protein targeting (21%).
...
PMID:Proteomic analysis of human osteoarthritic chondrocytes reveals protein changes in stress and glycolysis. 1818 17