Concentrations of Indoleamine Metabolic Intermediates in the Ventricular Cerebrospinal Fluid of Advanced Parkinson's Patients With Severe Postural Instability and Gait Disorders.

Iacono R. P., et al.
Journal of neural transmission, 1997

Abstract

Postural instability and gait disorders (PIGD) are the primary causes of disability in many but not all advanced Parkinson's disease (PD) patients. We have measured the concentrations of serotonin, 5-hydroxytryptophan (5-HTP), 5-hydroxy-3-indoleacetic acid (5-HIAA), and homovanillic acid (HVA) in samples of ventricular cerebrospinal fluid from ten PD patients with severe disability from PIGD and from ten PD patients with tremor and levodopa induced dyskinesia as their predominant motor dysfunction. The two groups were prospectively matched for duration of disease and age. No significant differences between the two groups were found in the concentration (mean +/- SD in ng/ml, PIGD dominant vs. tremor-dyskinesia dominant) of 5-HIAA (106 +/- 50 vs. 99 +/- 34) or HVA (1,068 +/- 595 vs. 881 +/- 469). Serotonin concentration was significantly lower (0.7 +/- 0.5 vs. 1.5 +/- 0.9) and 5-HTP concentration was substantially higher (684 +/- 1,054 vs. 6 +/- 5) in the patient group with PIGD as their predominant symptoms. Thus, the distinguishing feature of patients with severe PIGD appears to be a derangement in indoleamine metabolism at the reaction step catalyzed by aromatic amino acid decarboxylase (AADC). These findings suggest that aggravation of PIGD in advanced Parkinson's may be related in part to impaired serotonergic transmission secondary to inhibition or down regulation of AADC.

PMID:9295177
DOI:10.1007/BF01277663
Category:General properties of 5-Hydroxytryptophan

Articles similar to "Concentrations of Indoleamine Metabolic Intermediates in the Ventricular Cerebrospinal Fluid of Advanced Parkinson's Patients With Severe Postural Instability and Gait Disorders."

  • The properties of 5-Hydroxytryptophan: Aromatic L-amino Acid Decarboxylase Enzyme Activity in Deficient Patients and Heterozygotes. ( Aromatic L-amino acid decarboxylase (AADC) deficiency is a rare autosomal recessive disorder characterised by developmental delay, motor retardation and autonomic dysfunction... The presently described assays for AADC activity measurement allow an efficient, reproducible and non-invasive way to confirm the diagnosis of AADC deficiency. Since AADC enzyme activity is much higher with L-dopa as a substrate, this method is to be preferred over activity measurement with 5-HTP as a substrate for diagnostic purposes.)
  • The properties of 5-Hydroxytryptophan: Serotonin a La Carte: Supplementation With the Serotonin Precursor 5-hydroxytryptophan. (This paper reviews the preclinical and clinical evidence regarding the use of the dietary supplement 5-hydroxytryptophan (5-HTP) for the treatment of depression... The presently described assays for AADC activity measurement allow an efficient, reproducible and non-invasive way to confirm the diagnosis of AADC deficiency. Since AADC enzyme activity is much higher with L-dopa as a substrate, this method is to be preferred over activity measurement with 5-HTP as a substrate for diagnostic purposes.)
  • The properties of 5-Hydroxytryptophan: Stimulation of 5-HT2C Receptors Improves Cognitive Deficits Induced by Human Tryptophan Hydroxylase 2 Loss of Function Mutation. (Polymorphisms in the gene encoding the serotonin synthesis enzyme Tph2 have been identified in mental illnesses, including bipolar disorder, major depression, autism, schizophrenia, and ADHD... The presently described assays for AADC activity measurement allow an efficient, reproducible and non-invasive way to confirm the diagnosis of AADC deficiency. Since AADC enzyme activity is much higher with L-dopa as a substrate, this method is to be preferred over activity measurement with 5-HTP as a substrate for diagnostic purposes.)

Previous article

Tryptophan toxicity—time and dose response in rats. In: Tryptophan, Serotonin, and Melatonin.

Next article

Aromatic L-amino Acid Decarboxylase Enzyme Activity in Deficient Patients and Heterozygotes.