Systemic amyloidosis

Kyle, Robert A.; Gertz, Morie A.

doi:10.1016/1040-8428(90)90021-j

Cited by 75 publications

(44 citation statements)

References 367 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Carpal tunnel syndrome occurs in 21% of patients with AL 13,14,15 and should alert the physician to the possibility of this diagnosis, especially when associated with peripheral neuropathy. Patients 1 and 2 had neurophysiologic evidence of CTS prior to the onset of peripheral neuropathy.…”

Section: Discussionmentioning

confidence: 99%

Atypical presentations of primary amyloid neuropathy

2003

View full text Add to dashboard Cite

Primary amyloidosis (AL) may be complicated by peripheral neuropathy in 15-35% of cases. We report on four patients with atypical neurological presentations of AL neuropathy, whose diagnoses were delayed due to varied clinical presentations. The clinical presentation included painful sensory neuropathy (two patients), mononeuropathy multiplex (one patient), and primary demyelinating polyneuropathy (one patient). The latter two types of presentation have not been reported previously. The diagnosis was established by fat pad biopsy in two patients, lymph node biopsy in one, and sural nerve biopsy in one. Two patients were treated with high-dose melphalan followed by stem cell rescue, and one was treated with oral melphalan and prednisone. All three cases experienced stabilization of neuropathic symptoms. We report these cases in order to raise awareness of the varied clinical presentation of AL neuropathy.

show abstract

Section: Discussionmentioning

confidence: 99%

Atypical presentations of primary amyloid neuropathy

2003

View full text Add to dashboard Cite

show abstract

“…The diagnosis of AL-amyloidosis requires histologic demonstration of amyloid. Because a combination of fat aspirate and bone marrow biopsy is diagnostic in 90% of patients, fat aspiration is recommended as the initial diagnostic procedure, followed by bone marrow biopsy (100,102,103). If these studies are negative, then a renal biopsy is diagnostic in Ͼ95% of patients with clinical evidence of renal disease (97,100).…”

Section: Al-amyloidosismentioning

confidence: 99%

Multiple Myeloma

Korbet¹,

Schwartz²

2006

Journal of the American Society of Nephrology

160

149

View full text Add to dashboard Cite

“…Immunocyte-derived amyloid light chain (AL) (primary) amyloidosis is the most common form of systemic amyloidosis and, of all the amyloidoses, is associated with the shortest survival rate (1). In the majority of cases, this disease is associated with a nonmalignant expansion of a single plasma cell clone.…”

mentioning

confidence: 99%

Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation.

Schormann

Murrell

Liepnieks

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

An immunoglobulin light chain protein was isolated from the urine of an individual (BRE) with systemic amyloidosis. Complete amino acid sequence of the variable region of the light chain (VL) protein established it as a kappa I, which when compared with other kappa I amyloid associated proteins had unique residues, including Ile-34, Leu-40, and Tyr-71. To study the tertiary structure, BRE VL was expressed in Escherichia coli by using a PCR product amplified from the patient BRE's bone marrow DNA. The PCR product was ligated into pCZ11, a thermal-inducible replication vector. Recombinant BRE VL was isolated, purified to homogeneity, and crystallized by using ammonium sulfate as the precipitant. Two crystal forms were obtained. In crystal form I the BRE VL kappa domain crystallizes as a dimer with unit cell constants isomorphous to previously published kappa protein structures. Comparison with a nonamyloid VL kappa domain from patient REI, identified significant differences in position of residues in the hypervariable segments plus variations in framework region (FR) segments 40-46 (FR2) and 66-67 (FR3). In addition, positional differences can be seen along the two types of local diads, corresponding to the monomer-monomer and dimer-dimer interfaces. From the packing diagram, a model for the amyloid light chain (AL) fibril is proposed based on a pseudohexagonal spiral structure with a rise of approximately the width of two dimers per 360 degree turn. This spiral structure could be consistent with the dimensions of amyloid fibrils as determined by electron microscopy.

show abstract

Systemic amyloidosis

Cited by 75 publications

References 367 publications

Atypical presentations of primary amyloid neuropathy

Atypical presentations of primary amyloid neuropathy

Multiple Myeloma

Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation.

Contact Info

Product

Resources

About