Surgeons


Dunbar Broadway
601 N Caroline St
Ste 3231
Baltimore, MD 21278
410-955-6406
Locations and availability (1)

Awards & Distinctions ?

Awards  
Patients' Choice Award (2008 - 2009, 2013)

Publications & Research

Dr. Karami has contributed to 3 publications.
Title Effect of Food Deprivation and Hormones of Glucose Homeostasis on the Acetyl Coa Carboxylase Activity in Mouse Brain: a Potential Role of Acc in the Regulation of Energy Balance.
Date July 2007
Journal Nutrition & Metabolism
Excerpt

We studied the regulation of brain acetyl CoA carboxylase (ACC) activity during food deprivation and under the influence of hormones of glucose homeostasis: glucagon and insulin. Mice were deprived of food and water for time periods of 1, 3, 6, 9, 12 and 24 hours and were then allowed to re-feed for 5, 30 and 60 minutes. Mice that were deprived for up to 6 h, and then re-fed for 60 min, consumed the same amount of food compared to the ad libitum (control) animals. However, after 9 h of deprivation, mice consumed only 50% of food present even after 1 h of re-feeding, compared to the controls. The ACC activity was measured in the whole mouse brain of controls and after 1, 3, 6, 9, 12, and 24 h of food deprivation. Brain extracts assayed from control mice expressed an ACC activity of 0.988 +/- 0.158 fmol/min/mg tissue without citrate and 0.941 +/- 0.175 fmol/min/mg tissue with citrate. After 1 h of food deprivation, the total ACC activity without citrate decreased to 0.575 +/- 0.087 fmol/min/mg and in the presence of citrate, 0.703 +/- 0.036 fmol/min/mg activity was measured. The citrate-dependent ACC activity decreased over time, with only 0.478 +/- 0.117 fmol/min/mg of activity remaining after 24 h. Intraperitoneal (i.p.) injections of insulin, glucagon and phosphate buffered saline (PBS) were performed and whole brain ACC activity measured. After hormone administration, there were no significant differences in ACC activity in the presence of citrate. However, in the absence of citrate, there was a significant 20% decrease in ACC activity with glucagon (1.36 +/- 0.09 fmol/min/mg) and a 33% increase with insulin (2.49 +/- 0.11 fmol/min/mg) injections compared to PBS controls (1.67 +/- 0.08 fmol/min/mg). Neuropeptide Y (NPY) levels of corresponding brain extracts were measured by ELISA (OD) using anti-NPY antibody and showed an 18% decrease upon insulin injection (0.093 +/- 0.019) and a 50% increase upon glucagon injection (0.226 +/- 0.084) as compared to controls injected with PBS (0.114 +/- 0.040). Thus, we postulate that the changes in ACC levels under metabolic conditions would result in a fluctuation of malonyl CoA levels, and subsequent modulation of NPY levels and downstream signaling.

Title Isolation, Partial Purification, and Characterization of a Novel Petromyzonol Sulfotransferase from Petromyzon Marinus (lamprey) Larval Liver.
Date November 2004
Journal Journal of Lipid Research
Excerpt

We have isolated, partially purified, and characterized the 5 alpha-petromyzonol (5 alpha-PZ), (5 alpha-cholan- 3 alpha, 7 alpha, 12 alpha, 24-tetrahydroxy-) sulfotransferase (PZ-SULT) from larval lamprey liver. Crude liver extracts exhibited a PZ-SULT activity of 0.9120 pmol/min/mg in juvenile and 12.62 pmol/min/mg in larvae. Using crude larval liver extracts and various 5 beta-cholan substrates and allocholic acid there was negligible activity, however, with 5 alpha-PZ and 3-keto-5 alpha-PZ the SULT activity was 231.5 pmol/min/mg and 180.8 pmol/min/mg respectively. This established that the sulfotransferase of lamprey larval liver extracts prefers (5 alpha) substrates and it is selective for hydroxyl at C-24. PZ-SULT was purified through various chromatography procedures. Partially purified PZ-SULT exhibited a pH optimum of 8.0, a temperature optimum of 22 degrees C, and activity was linear for 1h. PZ-SULT exhibited a K(m) of 2.5 microM for PAPS and a K(m) of 8 microM for PZ. The affinity purified peak PZ-SULT exhibited a specific activity of 2,038 pmol/min/mg. The peak protein upon SDS-PAGE, correlated to an Mw 47 kDa. Photoaffinity labeling with PAP(35)S, specifically crosslinked the 47 kDa protein, further confirming the identity of PZ-SULT. Partial amino acid sequencing of the putative 47 kDa PZ-SULT protein yielded a peptide sequence (M)SISQAVDAAFXEI, which possessed an overall (approximately 35-40%) homology with mammalian SULT2B1a.

Title Malignant Peripheral Nerve Sheath Tumor of the Vestibulocochlear Nerve and Brainstem: Multimodality Treatment with Survival of 27 Months. A Case Report and Review of the Literature.
Date
Journal Neurosurgery
Excerpt

Malignant peripheral nerve sheath tumors are the most common malignant mesenchymal tumors of soft tissues, but they are very rare when found to arise from a cranial nerve and when not in association with neurofibromatosis. These tumors are highly malignant and carry a poor prognosis with survival usually less than 6 months.


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