1.Epiploic Appendagitis: An uncommon surgical diagnosis
Michael Arvind ; Zakry Yahya ; Hanif Hussein
The Medical Journal of Malaysia 2017;72(2):128-129
Epiploic appendagitis or appendices epiploicae, is a rare
cause of abdominal pain in patients with mild signs of
abdominal pathology. It mimics diverticulitis or appendicitis
clinically as there are no pathognomonic features. It is a
surgical diagnosis presenting with localised, sharp, acute
abdominal pain, not associated with symptoms like nausea,
vomiting, fever or suggestive laboratory values. With the
availability of abdominal CT scans and ultrasound, it will
frequently be a differential diagnosis preventing
unnecessary surgery for patients. However, it may be
erroneous and therefore clinical judgement is of paramount
importance. This report highlights this rare presentation and
identifies management guidelines.
KEY WORDS:
Epiploic appendagitis; Appendices epiploicae; Appendicitis;
Diverticulitis
2.Fulminant necrotising amoebic colitis: A diagnostic conundrum
Michael Arvind ; Jasjit Singh Nijhar ; Prabhu Ramasamy
The Medical Journal of Malaysia 2015;70(6):365-367
Fulminant necrotising amoebic colitis is a complication of
untreated amoebiasis. This is seen in mainly low-income
countries. It has a high mortality rate and is difficult to
diagnose. We present an extremely rare case of fulminant
necrotising amoebic colitis that caused diagnostic
confusion in mimicking an acute abdomen, presumably
caused by a perforated duodenal ulcer.
3.Computed tomography of the thorax with 3D reconstruction in penetrating chest injury
Michael Arvind ; Zakry Yahya ; Razali Ibrahim ; Hanif Hussein
The Medical Journal of Malaysia 2017;72(1):75-76
Penetrating chest wounds is less common but more deadly
then blunt trauma. Majority of penetrating chest trauma can
be managed conservatively with observation and simple
thoracotomy. This case report highlights a bizarre
occupational hazard causing a penetrating chest injury and
the option of non-invasive management with the aid of
computed tomography with 3D reconstruction.
Thoracic Injuries
4.A curious case of Meckel’s diverticulum
Michael Arvind ; Benedict Dharmaraj ; Mohd Razali Ibrahim ; Jasjit Singh Nijhar ; Zainal Ariffin Azizi
The Medical Journal of Malaysia 2016;71(4):203-204
Meckel’s diverticulitis or Meckel’s associated pathology
frequently presents in childhood with gastrointestinal
bleeding. It is rarely seen in adults. It is a congenital
abnormality that commonly goes undetected. We present a
case of a perforated Meckel’s diverticulum due to fishbone
ingestion in an elderly gentleman. The aim of this case
report is to highlight the rare presentation of a perforation in
a Meckel’s diverticulum due to an extrinsic pathology and to
outline diagnostic and management options in cases of
Meckel’s diverticulum.
Meckel Diverticulum
5.Specific interaction of hepatitis C virus glycoproteins with mannan binding lectin inhibits virus entry.
Kristelle S BROWN ; Michael J KEOGH ; Ania M OWSIANKA ; Richard ADAIR ; Arvind H PATEL ; James N ARNOLD ; Jonathan K BALL ; Robert B SIM ; Alexander W TARR ; Timothy P HICKLING
Protein & Cell 2010;1(7):664-674
Mannan-binding lectin (MBL) is a soluble innate immune protein that binds to glycosylated targets. MBL acts as an opsonin and activates complement, contributing to the destruction and clearance of infecting microorganisms. Hepatitis C virus (HCV) encodes two envelope glycoproteins E1 and E2, expressed as non-covalent E1/E2 heterodimers in the viral envelope. E1 and E2 are potential ligands for MBL. Here we describe an analysis of the interaction between HCV and MBL using recombinant soluble E2 ectodomain fragment, the full-length E1/E2 heterodimer, expressed in vitro, and assess the effect of this interaction on virus entry. A binding assay using antibody capture of full length E1/E2 heterodimers was used to demonstrate calcium dependent, saturating binding of MBL to HCV glycoproteins. Competition with various saccharides further confirmed that the interaction was via the lectin domain of MBL. MBL binds to E1/E2 representing a broad range of virus genotypes. MBL was shown to neutralize the entry into Huh-7 cells of HCV pseudoparticles (HCVpp) bearing E1/E2 from a wide range of genotypes. HCVpp were neutralized to varying degrees. MBL was also shown to neutralize an authentic cell culture infectious virus, strain JFH-1 (HCVcc). Furthermore, binding of MBL to E1/E2 was able to activate the complement system via MBL-associated serine protease 2. In conclusion, MBL interacts directly with HCV glycoproteins, which are present on the surface of the virion, resulting in neutralization of HCV particles.
Binding, Competitive
;
Glycosylation
;
Hepacivirus
;
genetics
;
pathogenicity
;
physiology
;
Humans
;
Mannose-Binding Lectin
;
metabolism
;
Mannose-Binding Protein-Associated Serine Proteases
;
metabolism
;
Monosaccharides
;
metabolism
;
Protein Binding
;
Protein Multimerization
;
Tumor Cells, Cultured
;
Viral Envelope Proteins
;
metabolism
;
Virion
;
pathogenicity
;
physiology
;
Virus Internalization