Chandra D

References (3)

Title : Serum Amylase and Lipase Estimation in Diabetic Ketoacidosis - Chandra_2022_J.Assoc.Physicians.India_70_11
Author(s) : Chandra D , Bsavaraju M , Mr R , Av A , R S
Ref : J Assoc Physicians India , 70 :11 , 2022
Abstract : Diabetic ketoacidosis is one of the hyperglycemic emergencies, there is insulin deficiency coupled with concomitant elevation of counter regulatory hormones. This hormonal imbalance promotes gluconeogenesis, glycolysis, glycogenolysis, protein breakdown and lipolysis.The symptoms of DKA like nausea, vomiting, epigastric pain can be present in acute pancreatitis also. From various studies it has been identified that in DKA, non specific elevation of serum amylase and lipase levels occurs in 16-25% of cases. Elevation of serum amylase, and lipase levels in association with severe abdominal pain often trigger the initial diagnosis of acute pancreatitis. So this study was carried out to study the elevation of serum amylase and lipase levels in patients with DKA. MATERIAL: This cross sectional study was conducted in department of medicine KR Hospital,Mysore medical college and research institute, mysore during the study period of six months from June 2021 to november 2021. A total of 50 patients were included in the study after fulfilling the inclusion and exclusion criteria. OBSERVATION: Among 50 cases studied, 9 cases (18%) with DKA are showing elevation of serum amylase levels and 13 cases(26%) of cases are showing elevation of serum lipase,34 cases(68%) were males and 16 cases(32%) were female. Among the 50 cases studied,infection is the most precipitating factor seen in 34cases (68%),followed by omission of insulin in 12 cases(24%), unidentified cause in 4 cases(8%). CONCLUSION: significant elevation of serum amylase and serum lipase which are more specific for diagnosis of acute pancreatitis can also be seen in patients with diabetic ketoacidosis. Elevated serum amylase and lipase can occur in patients with DKA probably due to metabolic derangements,decreased clearance of enzymes and not due to acute pancreatitis The clinician must take these data into account when evaluating abdominal symptoms in DKA patients.
ESTHER : Chandra_2022_J.Assoc.Physicians.India_70_11
PubMedSearch : Chandra_2022_J.Assoc.Physicians.India_70_11
PubMedID: 35443366

Title : Profiling Active Enzymes for Polysorbate Degradation in Biotherapeutics by Activity-Based Protein Profiling - Li_2021_Anal.Chem_93_8161
Author(s) : Li X , Chandra D , Letarte S , Adam GC , Welch J , Yang RS , Rivera S , Bodea S , Dow A , Chi A , Strulson CA , Richardson DD
Ref : Analytical Chemistry , 93 :8161 , 2021
Abstract : Polysorbate is widely used to maintain stability of biotherapeutic proteins in pharmaceutical formulation development. Degradation of polysorbate can lead to particle formation in drug products, which is a major quality concern and potential patient risk factor. Enzymatic activity from residual host cell enzymes such as lipases and esterases plays a major role for polysorbate degradation. Their high activity, often at very low concentration, constitutes a major analytical challenge in the biopharmaceutical industry. In this study, we evaluated and optimized the activity-based protein profiling (ABPP) approach to identify active enzymes responsible for polysorbate degradation. Using an optimized chemical probe, we established the first global profile of active serine hydrolases in harvested cell culture fluid (HCCF) for monoclonal antibodies (mAbs) production from two Chinese hamster ovary (CHO) cell lines. A total of eight known lipases were identified by ABPP with enzyme activity information, while only five lipases were identified by a traditional abundance-based proteomics (TABP) approach. Interestingly, phospholipase B-like 2 (PLBL2), a well-known problematic HCP was not found to be active in process-intermediates from two different mAbs. In a proof-of-concept study with downstream samples, phospholipase A2 group VII (PLA2G7) was only identified by ABPP and confirmed to contribute to polysorbate-80 degradation for the first time. The established ABBP approach is approved to be able to identify low-abundance host cell enzymes and fills the gap between lipase abundance and activity, which enables more meaningful polysorbate degradation investigations for biotherapeutic development.
ESTHER : Li_2021_Anal.Chem_93_8161
PubMedSearch : Li_2021_Anal.Chem_93_8161
PubMedID: 34032423
Gene_locus related to this paper: human-PLA2G7

Title : LipC (Rv0220) is an immunogenic cell surface esterase of Mycobacterium tuberculosis - Shen_2012_Infect.Immun_80_243
Author(s) : Shen G , Singh K , Chandra D , Serveau-Avesque C , Maurin D , Canaan S , Singla R , Behera D , Laal S
Ref : Infect Immun , 80 :243 , 2012
Abstract : We have reported previously the identification of novel proteins of Mycobacterium tuberculosis by the immunoscreening of an expression library of M. tuberculosis genomic DNA with sera obtained from M. tuberculosis-infected rabbits at 5 weeks postinfection. In this study, we report the further characterization of one of these antigens, LipC (Rv0220). LipC is annotated as a member of the Lip family based on the presence of the consensus motif "GXSXG" characteristic of esterases. Although predicted to be a cytoplasmic enzyme, we provide evidence that LipC is a cell surface protein that is present in both the cell wall and the capsule of M. tuberculosis. Consistent with this localization, LipC elicits strong humoral immune responses in both HIV-negative (HIV-) and HIV-positive (HIV+) tuberculosis (TB) patients. The absence of anti-LipC antibodies in sera from purified protein derivative-positive (PPD+) healthy subjects confirms its expression only during active M. tuberculosis infection. Epitope mapping of LipC identified 6 immunodominant epitopes, 5 of which map to the exposed surface of the modeled LipC protein. The recombinant LipC (rLipC) protein also elicits proinflammatory cytokine and chemokine responses from macrophages and pulmonary epithelial cells. rLipC can hydrolyze short-chain esters with the carbon chain containing 2 to 10 carbon atoms. Together, these studies demonstrate that LipC is a novel cell surface-associated esterase of M. tuberculosis that is highly immunogenic and elicits both antibodies and cytokines/chemokines.
ESTHER : Shen_2012_Infect.Immun_80_243
PubMedSearch : Shen_2012_Infect.Immun_80_243
PubMedID: 22038913
Gene_locus related to this paper: myctu-Rv0220