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This version published online on September 30, 2004
Endocrinology, doi:10.1210/en.2004-0780
A more recent version of this article appeared on December 1, 2004
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Submitted on June 22, 2004
Accepted on September 24, 2004

Unraveling the Amyloid Associated with Human Medullary Thyroid Carcinoma#

Ritu Khurana*, Amit Agarwal, Virendra K. Bajpai, Nidhi Verma, Ashok K. Sharma, Ram P. Gupta, and Kunnath P. Madhusudan

Molecular and Structural Biology Division, Electron Microscopy Unit, Sophisticated Analytical Instrument Facility, Central Drug Research Institute, Chattar Manzil Building, Lucknow, 226001 India; Department of Endocrine Surgery, Sanjay Gandhi Post Graduate Institute, Lucknow, India; Central Electronics and Engineering Research Institute, Pilani, India

* To whom correspondence should be addressed. E-mail: rkhurana{at}ccmb.res.in.

Medullary thyroid carcinoma is associated with amyloid deposition in the surrounding tissues. Medullary thyroid carcinoma positive tumor thyroid tissues surgically removed from patients were used in our study to extract amyloid. We tested the medullary thyroid carcinoma extracts for the presence of amyloid by measuring fold enhancement of thioflavin T fluorescence. Transmission electron microscopic study and atomic force microscopy of medullary thyroid carcinoma patient extracts revealed typical amyloid fibrils. Matrix assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric analysis demonstrated full length calcitonin as the constituent of the medullary thyroid carcinoma amyloid from seven patients as opposed to the alternately processed prohormone of calcitonin suggested by Sletton and coworkers (Sletton et al. 1976 J. Exp. Med. 143: 993-998). Our results unequivocally demonstrated that full-length calcitonin is the sole constituent of amyloid in medullary thyroid carcinoma.
Key words: Calcitonin amyloidosis • Tumor associated amyloid • AMCT • MTC • Mass Spectrometry • matrix assisted laser desorption ionization - time of flight mass spectrometry • MALDI-TOFMS • Transmission electron microscopy • atomic force microscopy




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