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Article: Correction to: Femoral Shaft Fracture in Post-polio Syndrome Patients: Case Series from a Level-I Trauma Center and Review of Literature.

Gupta, Anupam / Saurabh, Suman / Trikha, Tanya / Karpe, Aashraya / Mittal, Samarth

2022 Volume 57, Issue 1, Page(s) 166

Abstract: This corrects the article DOI: 10.1007/s43465-022-00683-8.]. ...

Abstract	[This corrects the article DOI: 10.1007/s43465-022-00683-8.].
Language	English
Publishing date	2022-11-29
Publishing country	Switzerland
Document type	Published Erratum
ZDB-ID	603194-8
ISSN	0019-5413
ISSN	0019-5413
DOI	10.1007/s43465-022-00764-8
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Article: Femoral Shaft Fracture in Post-polio Syndrome Patients: Case Series from a Level-I Trauma Center and Review of Literature.

Gupta, Anupam / Saurabh, Suman / Trikha, Tanya / Karpe, Aashraya / Mittal, Samarth

Indian journal of orthopaedics

2022 Volume 56, Issue 8, Page(s) 1339–1346

Abstract: Background: Femoral shaft fracture in patients of post-polio syndrome (PPS) represents an uncommon yet complex injury pattern. Poorly developed soft-tissue envelope, decreased muscle bulk, reduced vascularity, regional osteopenia, joint contractures, ... ...

Abstract	Background: Femoral shaft fracture in patients of post-polio syndrome (PPS) represents an uncommon yet complex injury pattern. Poorly developed soft-tissue envelope, decreased muscle bulk, reduced vascularity, regional osteopenia, joint contractures, and altered bony anatomy impose significant surgical challenges. Thorough pre-operative planning is imperative as each case requires individualized approach and method of fixation. The aim of the study was to analyze the clinical outcomes in such patients following fracture fixation and to assess the surgical challenges encountered and provide solutions. Materials and methods: A retrospective case series of 33 patients with femoral shaft fracture in PPS limbs was undertaken. Mode of injury, method of fixation, surgical time, intra-operative blood loss, union time, and complications were recorded. Results: Low-energy fall was the most common mechanism of injury (73%). Thirty-three patients underwent fixation with intramedullary nailing being the most common mode (79%). Femoral canal diameter, femoral bow, fracture location and morphology and clinical deformities of the patients are key governing factors that determine the choice of implant. Locking plates, pre-contoured anatomical plates, and titanium elastic nailing system offer an alternative in patients unsuitable for nailing. With no difference between various implants, average time for bone healing was 13.8 ± 4.4 weeks. All patients resumed full weight-bearing mobilization and returned to pre-injury activity status at the end of 6 months post-surgery. Conclusion: With detailed pre-operative work-up, contemplating intra-operative difficulties, individualized surgical plan, careful handling of soft tissues, and availability of back-up implants, good clinical outcomes can be achieved in femur fractures in PPS patients.
Language	English
Publishing date	2022-06-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	603194-8
ISSN	0019-5413
ISSN	0019-5413
DOI	10.1007/s43465-022-00683-8
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Article: Technical tip for removal of broken cephalomedullary reamer tip in cases of proximal femoral nailing.

Kumar, Arvind / Jain, Aditya / Saurabh, Suman / Trikha, Vivek / Mittal, Samarth

Journal of clinical orthopaedics and trauma

2019 Volume 10, Issue 5, Page(s) 969–971

Abstract: Instrumentation breakage around hip joint can pose a challenging situation considering its vicinity to several vital structures. Broken fragments carry the risk of migration and thus should be removed as early as possible. A case of successful retrieval ... ...

Abstract	Instrumentation breakage around hip joint can pose a challenging situation considering its vicinity to several vital structures. Broken fragments carry the risk of migration and thus should be removed as early as possible. A case of successful retrieval of broken tip of cephalomedullary lag screw reamer of a cephalomedullary nail, in basicervical region of femoral neck, during fixation of a subtrochanteric femoral fracture has been reported. Literature review has been done to suggest techniques to tackle similar situations using simple and commonly available instruments.
Language	English
Publishing date	2019-01-15
Publishing country	India
Document type	Case Reports
ZDB-ID	2596956-0
ISSN	2213-3445 ; 0976-5662
ISSN (online)	2213-3445
ISSN	0976-5662
DOI	10.1016/j.jcot.2019.01.014
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Thesis ; Online: Unraveling the Molecular Mechanisms of Human Amylin Binding, Turnover and Toxicity in Pancreatic Cells

Trikha, Saurabh

2013

Abstract: Islet amyloid polypeptide or amylin is a recently discovered 37 amino acid residue signaling protein (hormone) that is produced and co-secreted along with insulin by pancreatic beta-cells. In late onset of diabetes, amylin readily aggregates forming ... ...

Abstract	Islet amyloid polypeptide or amylin is a recently discovered 37 amino acid residue signaling protein (hormone) that is produced and co-secreted along with insulin by pancreatic beta-cells. In late onset of diabetes, amylin readily aggregates forming protein deposits or plaques that are toxic to beta-cells, resulting in beta-cell apoptosis. Given the well-known role of cholesterol and lipids in etiology of diabetes, I explored whether these two essential PM components regulate amylin assembly and aggregation on artificial (synthetic) membranes. Using high resolution imaging and spectroscopic approaches, I demonstrated that amylin undergoes facilitated aggregation and conformational changes in the presence of membranes composed of anionic lipids such as phosphatidylserine (PS). The presence of cholesterol on the other hand inhibited lipid-induced aggregation of amylin in solution and on model planar membranes. However, the patho-physiological consequence of cholesterol-regulated amylin polymerization on membranes, and biochemical mechanisms that protect beta-cells from amylin toxicity are poorly understood. Hence, in my subsequent study, I reported that PM cholesterol plays a key role in molecular recognition, sorting and internalization of toxic amylin oligomers but not monomers in pancreatic rat insulinoma and human islet cells. Depletion of PM cholesterol or the disruption of the cytoskeleton network inhibited internalization of amylin oligomers, which in turn enhanced extracellular oligomer accumulation and potentiated amylin toxicity. In contrast to oligomers, amylin monomers followed clathrin-dependent endocytosis, which was not sensitive to cholesterol depletion. Our studies identified an actin-mediated and cholesterol-dependent mechanism for selective uptake and clearance of amylin oligomers, impairment of which greatly potentiated amylin toxicity. However, the exact uptake mechanism and trafficking routes of these molecular forms and their significance for amylin toxicity are yet to be determined. Hence, in my further study, I observed that pancreatic cells employed different strategies to eliminate amylin's toxic and non-toxic molecular forms. My study also revealed that macropinocytosis serves a major cyto-protective role in these cells, by clearing of amylin molecular forms. The overreaching goal was to fully elucidate the internalization and trafficking pathways of human amylin monomers and toxic oligomers in pancreatic cells.
Keywords	Biology\|Cellular biology\|Biophysics
Subject code	500
Language	ENG
Publishing date	2013-01-01 00:00:01.0
Publisher	The George Washington University
Publishing country	us
Document type	Thesis ; Online
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Article ; Online: Long-term outcomes in Primary congenital glaucoma, aniridia and anterior segment dysgenesis.

Magan, Tejal / Tanner, Alexander / Fajardo-Sanchez, Julia / Lim, Kin Sheng / Goyal, Saurabh / Rodrigues, Ian / Amaya, Luis / Trikha, Sameer / Kulkarni, Avinash / Hammond, Christopher / Lascaratos, Gerassimos / Yu-Wai-Man, Cynthia

European journal of ophthalmology

2022 Volume 32, Issue 5, Page(s) 2920–2927

Abstract: Aim: To determine the long-term outcomes of a cohort of complex patients with primary congenital glaucoma, aniridia and anterior segment dysgenesis.: Methods: Retrospective consecutive series between 1990-2021 in two UK tertiary centres: Guy's and St ...

Abstract	Aim: To determine the long-term outcomes of a cohort of complex patients with primary congenital glaucoma, aniridia and anterior segment dysgenesis. Methods: Retrospective consecutive series between 1990-2021 in two UK tertiary centres: Guy's and St Thomas' NHS Foundation Trust and King's College Hospital NHS Foundation Trust. We recorded the number and types of surgical and laser treatments along with preoperative and postoperative data, including intraocular pressures (IOP) and anti-glaucoma medications. Results: A total of 41 eyes of 21 patients were included. Primary diagnoses were primary congenital glaucoma in 16 eyes (39.0%), aniridia in 14 eyes (34.2%), and anterior segment dysgenesis in 8 eyes (19.5%). Sixteen eyes (39.0%) had one or more glaucoma surgery or laser procedures for advanced glaucoma, and the long-term follow-up was 12.8 ± 3.6 years. There was a significant decrease in postoperative IOP (mmHg) at 3 months (16.5 ± 1.6; Conclusions: Surgical management of these complex eyes with advanced glaucoma is challenging. Overall, the cohort had good surgical outcomes with a significant decrease in IOP by 36.1% after long-term follow-up.
MeSH term(s)	Aniridia/surgery ; Eye Abnormalities ; Follow-Up Studies ; Glaucoma/drug therapy ; Humans ; Intraocular Pressure ; Retrospective Studies ; Trabeculectomy/adverse effects ; Treatment Outcome ; Visual Acuity
Language	English
Publishing date	2022-01-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	1089461-5
ISSN	1724-6016 ; 1120-6721
ISSN (online)	1724-6016
ISSN	1120-6721
DOI	10.1177/11206721211073208
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Article ; Online: Distinct internalization pathways of human amylin monomers and its cytotoxic oligomers in pancreatic cells.

Trikha, Saurabh / Jeremic, Aleksandar M

PloS one

2013 Volume 8, Issue 9, Page(s) e73080

Abstract: Toxic human amylin oligomers and aggregates are implicated in the pathogenesis of type 2 diabetes mellitus (TTDM). Although recent studies have shown that pancreatic cells can recycle amylin monomers and toxic oligomers, the exact uptake mechanism and ... ...

Abstract	Toxic human amylin oligomers and aggregates are implicated in the pathogenesis of type 2 diabetes mellitus (TTDM). Although recent studies have shown that pancreatic cells can recycle amylin monomers and toxic oligomers, the exact uptake mechanism and trafficking routes of these molecular forms and their significance for amylin toxicity are yet to be determined. Using pancreatic rat insulinoma (RIN-m5F) beta (β)-cells and human islets as model systems we show that monomers and oligomers cross the plasma membrane (PM) through both endocytotic and non-endocytotic (translocation) mechanisms, the predominance of which is dependent on amylin concentrations and incubation times. At low (≤ 100 nM) concentrations, internalization of amylin monomers in pancreatic cells is completely blocked by the selective amylin-receptor (AM-R) antagonist, AC-187, indicating an AM-R dependent mechanism. In contrast at cytotoxic (µM) concentrations monomers initially (1 hour) enter pancreatic cells by two distinct mechanisms: translocation and macropinocytosis. However, during the late stage (24 hours) monomers internalize by a clathrin-dependent but AM-R and macropinocytotic independent pathway. Like monomers a small fraction of the oligomers initially enter cells by a non-endocytotic mechanism. In contrast a majority of the oligomers at both early (1 hour) and late times (24 hours) traffic with a fluid-phase marker, dextran, to the same endocytotic compartments, the uptake of which is blocked by potent macropinocytotic inhibitors. This led to a significant increase in extra-cellular PM accumulation, in turn potentiating amylin toxicity in pancreatic cells. Our studies suggest that macropinocytosis is a major but not the only clearance mechanism for both amylin's molecular forms, thereby serving a cyto-protective role in these cells.
MeSH term(s)	Animals ; Biopolymers/metabolism ; Cell Line, Tumor ; Cells, Cultured ; Endocytosis ; Humans ; Islet Amyloid Polypeptide/metabolism ; Microscopy, Confocal ; Pancreas/cytology ; Pancreas/metabolism ; Rats ; Receptors, Islet Amyloid Polypeptide/metabolism
Chemical Substances	Biopolymers ; Islet Amyloid Polypeptide ; Receptors, Islet Amyloid Polypeptide
Language	English
Publishing date	2013-09-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0073080
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Article ; Online: Clinical Outcomes and Cost Analysis of PreserFlo versus Trabeculectomy for Glaucoma Management in the United Kingdom.

Van Lancker, Lauren / Saravanan, Amrita / Abu-Bakra, Mohammed / Reid, Kyle / Quijano, Claudia / Goyal, Saurabh / Rodrigues, Ian / Lascaratos, Gerassimos / Trikha, Sameer / Barwood, Caroline / Combe, Emily / Kulkarni, Avinash / Lim, Kin Sheng / Low, Sancy

Ophthalmology. Glaucoma

2022 Volume 6, Issue 4, Page(s) 342–357

Abstract: Purpose: Clinical evaluation and cost analysis of mitomycin-C-augmented PreserFlo MicroShunt versus trabeculectomy.: Design: Retrospective cohort study across 3 teaching hospitals.: Participants: A total of 134 consecutive eyes of 129 patients (70 ...

Abstract	Purpose: Clinical evaluation and cost analysis of mitomycin-C-augmented PreserFlo MicroShunt versus trabeculectomy. Design: Retrospective cohort study across 3 teaching hospitals. Participants: A total of 134 consecutive eyes of 129 patients (70 undergoing MicroShunt, 64 trabeculectomy). Methods: Primary and secondary glaucoma cases with uncontrolled intraocular pressure (IOP) were included. Neovascular glaucoma and surgery combined with cataract extraction were excluded. The cost analysis used results from the clinical study to estimate operative costs (equipment and staff costs) and postoperative costs (follow-up visits, nonglaucoma medications, and postoperative procedures) per eye for PreserFlo and trabeculectomy. Main outcome measures: The primary clinical outcome measure was surgical failure (defined as IOP > 21 mmHg or < 20% reduction from baseline, IOP ≤ 5 mmHg, reoperation, or loss of light perception) or qualified and complete success (with or without medication) at 18 months. Secondary measures were IOP, glaucoma medications, visual acuity, mean deviation, time to cessation of steroid drops, complications, surgical time, follow-up visits, postoperative interventions, and reoperations. The cost analysis evaluated costs of PreserFlo compared with trabeculectomy. Results: Baseline characteristics were similar, except for more non-White patients in the trabeculectomy group (51% Black and Asian vs. 32% MicroShunt, P = 0.02) and more cases with prior ab externo glaucoma surgery in the MicroShunt group (19% vs. 3% in the trabeculectomy group, P = 0.004). Overall, 59% of eyes had primary open-angle glaucoma. Mean follow-up was 19.9 months for both groups. At 18 months, surgical failure was 25% for MicroShunt compared with 35% for trabeculectomy (P = 0.18). Failure in MicroShunt cases was due to inadequate IOP reduction (84%) or reoperation for glaucoma (16%). Failure in trabeculectomy cases was due to inadequate IOP reduction (58%), persistent hypotony (29%), or reoperation for glaucoma (13%). Combined blebitis and endophthalmitis rate was 1.4% for MicroShunt and 3.1% for trabeculectomy. Cost analysis showed a savings of £245 to £566 per eye in the MicroShunt group, driven mostly by reduced postoperative procedures and follow-up visits. This is in contrast to prior randomized controlled trial data reporting the incremental cost of $2058 of PreserFlo over trabeculectomy. Conclusions: Our experience of introducing PreserFlo MicroShunt surgery showed it was safer than trabeculectomy and is a cost-saving and effective option that offers potential to free up highly limited National Health Service resources. Financial disclosure(s): Proprietary or commercial disclosure may be found after the references.
Language	English
Publishing date	2022-11-23
Publishing country	United States
Document type	Journal Article
ISSN	2589-4196
ISSN (online)	2589-4196
DOI	10.1016/j.ogla.2022.11.006
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Article: The Molecular Physiopathogenesis of Islet Amyloidosis.

Bhowmick, Diti Chatterjee / Singh, Sanghamitra / Trikha, Saurabh / Jeremic, Aleksandar M

Handbook of experimental pharmacology

2017 Volume 245, Page(s) 271–312

Abstract: Human islet amyloid polypeptide or amylin (hA) is a 37-amino acid peptide hormone produced and co-secreted with insulin by pancreatic β-cells. Under physiological conditions, hA regulates a broad range of biological processes including insulin release ... ...

Abstract	Human islet amyloid polypeptide or amylin (hA) is a 37-amino acid peptide hormone produced and co-secreted with insulin by pancreatic β-cells. Under physiological conditions, hA regulates a broad range of biological processes including insulin release and slowing of gastric emptying, thereby maintaining glucose homeostasis. However, under the pathological conditions associated with type 2 diabetes mellitus (T2DM), hA undergoes a conformational transition from soluble random coil monomers to alpha-helical oligomers and insoluble β-sheet amyloid fibrils or amyloid plaques. There is a positive correlation between hA oligomerization/aggregation, hA toxicity, and diabetes progression. Because the homeostatic balance between hA synthesis, release, and uptake is lost in diabetics and hA aggregation is a hallmark of T2DM, this chapter focuses on the biophysical and cell biology studies investigating molecular mechanisms of hA uptake, trafficking, and degradation in pancreatic cells and its relevance to h's toxicity. We will also discuss the regulatory role of endocytosis and proteolytic pathways in clearance of toxic hA species. Finally, we will discuss potential pharmacological approaches for specific targeting of hA trafficking pathways and toxicity in islet β-cells as potential new avenues toward treatments of T2DM patients.
MeSH term(s)	Amyloidosis/etiology ; Animals ; Diabetes Mellitus, Type 2/drug therapy ; Diabetes Mellitus, Type 2/etiology ; Endocytosis ; Humans ; Islet Amyloid Polypeptide/chemistry ; Islet Amyloid Polypeptide/physiology ; Islets of Langerhans/metabolism ; Proteasome Endopeptidase Complex/physiology ; Protein Aggregates
Chemical Substances	Islet Amyloid Polypeptide ; Protein Aggregates ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2017-10-18
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ISSN	0171-2004
ISSN	0171-2004
DOI	10.1007/164_2017_62
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Article ; Online: Distinct internalization pathways of human amylin monomers and its cytotoxic oligomers in pancreatic cells.

Saurabh Trikha / Aleksandar M Jeremic

PLoS ONE, Vol 8, Iss 9, p e

2013 Volume 73080

Abstract	Toxic human amylin oligomers and aggregates are implicated in the pathogenesis of type 2 diabetes mellitus (TTDM). Although recent studies have shown that pancreatic cells can recycle amylin monomers and toxic oligomers, the exact uptake mechanism and trafficking routes of these molecular forms and their significance for amylin toxicity are yet to be determined. Using pancreatic rat insulinoma (RIN-m5F) beta (β)-cells and human islets as model systems we show that monomers and oligomers cross the plasma membrane (PM) through both endocytotic and non-endocytotic (translocation) mechanisms, the predominance of which is dependent on amylin concentrations and incubation times. At low (≤ 100 nM) concentrations, internalization of amylin monomers in pancreatic cells is completely blocked by the selective amylin-receptor (AM-R) antagonist, AC-187, indicating an AM-R dependent mechanism. In contrast at cytotoxic (µM) concentrations monomers initially (1 hour) enter pancreatic cells by two distinct mechanisms: translocation and macropinocytosis. However, during the late stage (24 hours) monomers internalize by a clathrin-dependent but AM-R and macropinocytotic independent pathway. Like monomers a small fraction of the oligomers initially enter cells by a non-endocytotic mechanism. In contrast a majority of the oligomers at both early (1 hour) and late times (24 hours) traffic with a fluid-phase marker, dextran, to the same endocytotic compartments, the uptake of which is blocked by potent macropinocytotic inhibitors. This led to a significant increase in extra-cellular PM accumulation, in turn potentiating amylin toxicity in pancreatic cells. Our studies suggest that macropinocytosis is a major but not the only clearance mechanism for both amylin's molecular forms, thereby serving a cyto-protective role in these cells.
Keywords	Medicine ; R ; Science ; Q
Subject code	610
Language	English
Publishing date	2013-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: Proteasome regulates turnover of toxic human amylin in pancreatic cells.

Singh, Sanghamitra / Trikha, Saurabh / Sarkar, Anjali / Jeremic, Aleksandar M

The Biochemical journal

2016 Volume 473, Issue 17, Page(s) 2655–2670

Abstract: Toxic human amylin (hA) oligomers and aggregates are implicated in the pathogenesis of type 2 diabetes mellitus (T2DM). Although recent studies demonstrated a causal connection between hA uptake and toxicity in pancreatic cells, the mechanism of amylin's ...

Abstract	Toxic human amylin (hA) oligomers and aggregates are implicated in the pathogenesis of type 2 diabetes mellitus (T2DM). Although recent studies demonstrated a causal connection between hA uptake and toxicity in pancreatic cells, the mechanism of amylin's clearance following its internalization and its relationship to toxicity is yet to be determined, and hence was investigated here. Using pancreatic rat insulinoma β-cells and human islets as model systems, we show that hA, following its internalization, first accumulates in the cytosol followed by its translocation into nucleus, and to a lesser extent lysosomes, keeping the net cytosolic amylin content low. An increase in hA accumulation in the nucleus of pancreatic cells correlated with its cytotoxicity, suggesting that its excessive accumulation in the nucleus is detrimental. hA interacted with 20S core and 19S lid subunits of the β-cell proteasomal complex, as suggested by immunoprecipitation and confocal microscopy studies, which subsequently resulted in a decrease in the proteasome's proteolytic activity in these cells. In vitro binding and activity assays confirmed an intrinsic and potent ability of amylin to interact with the 20S core complex thereby modulating its proteolytic activity. Interestingly, less toxic and aggregation incapable rat amylin (rA) showed a comparable inhibitory effect on proteasome activity and protein ubiquitination, decoupling amylin aggregation/ toxicity and amylin-induced protein stress. In agreement with these studies, inhibition of proteasomal proteolytic activity significantly increased intracellular amylin content and toxicity. Taken together, our results suggest a pivotal role of proteasomes in amylin's turnover and detoxification in pancreatic cells.
MeSH term(s)	Animals ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Humans ; Islet Amyloid Polypeptide/metabolism ; Islet Amyloid Polypeptide/toxicity ; Microscopy, Confocal ; Pancreas/cytology ; Pancreas/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Rats
Chemical Substances	Islet Amyloid Polypeptide ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2016-09-01
Publishing country	England
Document type	Journal Article
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20160026
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