Expression of carbonic anhydrase isozymes (CA-I, CA-II, CA-III) during postnatal development of the rat gastrointestinal tract

Igarashi, Shigeru; Miura, Kohshi; Ichihara, Nobutsune; Kano, Yutaka; Nishita, Toshiho; Asari, Masao; Amasaki, H.

doi:10.1016/s0940-9602(96)80098-7

Cited by 3 publications

(3 citation statements)

References 16 publications

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“…CAIII is found almost exclusively in slow‐oxidative skeletal muscle fibers, in the epithelium of human esophagus, and in other tissues, but it has not yet been described in cells of the synovial membrane 19–27 . Carbonic anhydrase III is a cytosolic protein and belongs to a class of zinc‐binding metalloenzymes that catalyze the reversible hydration of carbonic dioxide and plays an essential role as an antioxidant agent 28 .…”

Section: Discussionmentioning

confidence: 99%

A New Target for Autoantibodies in Patients with Rheumatoid Arthritis

Robert-Pachot

Desbos

Moreira

et al. 2007

Annals of the New York Academy of Sciences

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Early treatment of rheumatoid arthritis (RA) with disease-modifying antirheumatic drugs can achieve a better disease outcome and reduce the severity of joint damage. The presence of autoantibodies in patient sera can precede onset of the disease and thus be predictive of the development of RA. To date, known autoantibodies in RA are positive in only 50-60% of RA patients at onset of disease and even less before the onset of any RA symptom. The aim of this study was to identify new antibodies that could be useful for the diagnosis of RA using synovial membrane proteins, which represent the best source of candidate RA autoantigens. The humoral reactivity of sera from RA patients was explored using immunoblotting on extracted proteins obtained from synovial membranes from RA after synovectomy or arthroplasty. A new target protein with a molecular weight of 26 kDa was found to be recognized by autoantibodies in RA sera. This protein was identified using MALDI-TOF mass spectrometry and two-dimensional electrophoresis as carbonic anhydrase III with a high level of confidence. In conclusion, this study demonstrates new autoantibodies in RA patients that are directed against carbonic anhydrase III. The sensitivity and specificity of these new autoantibodies for RA have to be further evaluated.

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Section: Discussionmentioning

confidence: 99%

A New Target for Autoantibodies in Patients with Rheumatoid Arthritis

Robert-Pachot

Desbos

Moreira

et al. 2007

Annals of the New York Academy of Sciences

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“…CA is a peptide with zinc (Zn) atom and several isoenzymes of CA family are isolated and characterized among animal species [1,10,12,17]. In 1952, the function of CA was firstly characterized by Janowitz [11] that it is associated with HCl excretion in gastric juice in mammals [11].…”

mentioning

confidence: 99%

“…CA can be detected by various methods such as the fluorescence antibody staining [9], immunohistochemistry [1,3,10,12], colorimetry [30] and pressure reducing method [16,18]. Based on previous studies, Kurata's method [15] is the most convenient with reasonable specificity and sensitivity.…”

mentioning

confidence: 99%

Distribution of Carbonic Anhydrase in Digestive Tract of Pond Loach (Misgurnus anguilicaudatus)

Chang

Chou

et al. 2006

The Journal of Veterinary Medical Science

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ABSTRACT. Carbonic anhydrase (CA) family is discovered in various species including mammals, avians and even plants, but it is rarely reported in fishes. Ten Pond Loaches were used in this study. The results indicated that no evidence of distribution of CA in esophagus. Nonetheless CA was found in the mucosal epithelium of stomach and in the villous epithelium of intestine demonstrated histochemically by the numerous black sedimentation of cobaltous sulfide (CoS) in these areas. In addition, black sedimentations of CoS were also found in all the vascular endothelium examined and red blood cells of digestive tract. The distribution of CA in Pond loach was more closely resemble amphibians than to other species, suggesting evolutional adaptation for Pond loach in aquatic environments. KEY WORDS: carbonic anhydrase, digestive tract, pond loach.

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Carbonic anhydrase III: A new target for autoantibodies in autoimmune diseases

et al. 2007

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The objective of this study was to identify new autoantibodies that could be useful for the diagnosis of rheumatoid arthritis (RA) using immunoblotting on synovial membrane proteins which represent the best source of candidate RA autoantigens. A new target protein with a molecular weight of 26 kDa was found to be recognized by autoantibodies in RA sera and was identified using MALDI-TOF mass spectrometry and second-dimension electrophoresis as carbonic anhydrase III (CAIII). Three similar protein spots at 26 kDa were recognized by both human sera and monoclonal antibody (mAb) directed against CAIII on immunoblotting using the human recombinant CAIII. Interestingly, CAIII expression within the synovial membrane was not observed in non-RA patients and was differentially expressed among RA patients. The sensitivity of these new autoantibodies for RA, using an immunoenzymatic technique, was 17%. Specificity was high when comparing non-autoimmune diseases (100%), while it was found to be weak (67%) when comparing some other autoimmune diseases, and particularly systemic lupus erythematosus (SLE). In conclusion, this study demonstrates that these new autoantibodies against CAIII are not restricted to RA. However the expression of CAIII in the synovial membrane of RA warrants further investigation of the pathophysiological relevance of this finding.

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Expression of carbonic anhydrase isozymes (CA-I, CA-II, CA-III) during postnatal development of the rat gastrointestinal tract

Cited by 3 publications

References 16 publications

A New Target for Autoantibodies in Patients with Rheumatoid Arthritis

A New Target for Autoantibodies in Patients with Rheumatoid Arthritis

Distribution of Carbonic Anhydrase in Digestive Tract of Pond Loach (Misgurnus anguilicaudatus)

Carbonic anhydrase III: A new target for autoantibodies in autoimmune diseases

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