 |
|
Is the Loose Anagen Hair Syndrome a Keratin Disorder?
A Clinical and Molecular Study
Valérie Chapalain, MD;
Hermelita Winter, PhD;
Lutz Langbein, PhD;
Jean-Michel Le Roy, MD;
Christine Labrèze, MD;
Milos Nikolic, MD;
Jürgen Schweizer, PhD;
Alain Taïeb, MD
Arch Dermatol. 2002;138:501-506.
ABSTRACT
| |
Objectives To report the clinical features of the loose anagen hair syndrome and
to test the hypothesis that the typical gap between the hair and the inner
root sheath may result from hereditary defects in the inner root sheath or
the apposed companion layer.
Design Case series.
Setting A pediatric dermatology unit (referral center).
Patients A consecutive sample of 17 children (13 girls). For 9 of them and their
first-degree relatives, molecular analyses were performed in the K6HF gene with 50 appropriate controls.
Intervention Minoxidil therapy (5% lotion) in 11 patients for 1 to 12 months.
Main Outcome Measures Clinical and follow-up features and determination of mutations in the K6HF gene.
Results Most patients had easily pluckable hair with no sign of scalp inflammation
or scarring. Ten patients seldom cut their hair, and 4 had unmanageable hair.
One patient had hypodontia. Two patients had an additional clinical phenotype
of diffuse partial woolly hair. The family history was positive for loose
anagen hair syndrome in 5 patients. Marked improvement was noted after treatment
with 5% minoxidil lotion in 7 of the 11 patients treated. Polymerase chain
reaction analysis of the gene segments encoding the  -helical 1A and
2B subdomains of K6hf, the type II cytokeratin exclusively expressed in the
companion layer, was performed in 9 families. In 3 of these 9 families, a
heterozygous glutamic acid and lysine mutation, E337K, was identified in the
L2 linker region of K6HF.
Conclusions Diffuse partial woolly hair can be associated with loose anagen hair
syndrome. A keratin mutation, E337K in K6HF, was possibly causative
in 3 of the 9 families studied. Another keratin, and possibly the type I partner
of K6hf, could be responsible for loose anagen hair syndrome in other patients,
or the gene involved may be a minor gene.
INTRODUCTION
SINCE 1990, it has been known that mutations in keratin genes can cause
various hereditary epithelial disorders. The deleterious mutations are not
randomly distributed along a keratin molecule, but occur preferentially in
those parts of the molecule that are essential for ordered filament formation.
The main areas involved in this process are the helix initiation motif or
the helix termination motif. The hereditary hair disease monilethrix can be
caused by a mutation in hair keratins.1
Loose anagen hair syndrome (LAHS) is a recently described hair disease,
characterized by easily pluckable hair. It was first reported by Zaun in 1984,2 and then by Nödl et al in 1986,3
and was then published in the US literature by Hamm and Traupe4
and Price and Gummer5 in 1989. The essential
finding is the ability, by gentle pulling, to painlessly extract anagen hairs
that lack the inner root sheath (IRS) and the outer root sheath.
Previous analyses of hair morphologic features in patients with LAHS
have shown that the main defect is a gap between the cuticle of the IRS and
the cuticle of the hair, without abnormalities of the hair follicle structure.
We hypothesized that the typical gap between the hair and the IRS may result
from defects in the IRS or in the apposed companion layer (CL). Both compartments
are tightly connected and are thought to stabilize the growing hair. Thus,
mutations in keratins expressed in these follicular compartments may compromise
the stable anchorage of the hair in the follicle. Unfortunately, the keratins
expressed in the different layers of the IRS are not known. In contrast, the
keratins expressed in the CL are known. The major keratin is the recently
discovered type II cytokeratin K6hf, which is exclusively expressed in the
CL.6 The other cytokeratins of the CL are keratin
pairs, K6a/K16 and K6b/K17.7 These keratin
pairs are also expressed in the outer root sheath and, therefore, mutations
in these keratins should result in disorders other than loose anagen.
We describe 17 consecutive patients with LAHS who were referred to our
department from January 1988 to December 1998. For 9 of them and their first-degree
relatives, molecular analyses were performed in the K6HF gene to look at possible causative mutations.
PATIENTS AND METHODS
PATIENTS
From January 1988 to December 1998, 17 cases of LAHS originating from
17 different families were diagnosed in our unit because of easily pluckable
hair, alopecia, and/or slow-growing hairs. The diagnosis was established on
clinical grounds associated with a trichogram in 16 patients. More than 50%
of dystrophic anagen hairs in the trichogram was considered as diagnostic
of LAHS in 14 of the 16 patients investigated.
DNA
After ethic committee approval, blood was drawn from consenting affected
and unaffected members of 9 nuclear families (the propositus and parents and
sometimes brothers and sisters) of this series and from 50 unrelated healthy
individuals, without a history of hair disorder, to whom the aim and nature
of the study had been explained. Genomic DNA was isolated (Blood and Tissue
Culture DNA Extraction System; QIAGEN GmbH, Hilden, Germany).
MUTATION ANALYSIS
The gene segments encoding the -helical 1A and 2B subdomains
of K6HF were amplified by the polymerase chain reaction
using the primer pairs 5'-TCAGTGGCCCCAGCTTCCCCTGTT-3' (forward
primer) and 5'-TGTTCCTCAGTTCAGCTTCAAGCCTGC-3' (reverse primer)
for amplification of the 1A region and the primer pairs 5'-GGCAGGCTTGAAGCTGAACTGAGGA-3'
(forward primer) and 5'-GGAGACAAACTTGACGCTAGAACCA-3' (reverse
primer) for amplification of the 2B region. Polymerase chain reaction analysis
was performed (Expand Long Template PCR System; Roche, Mannheim, Germany).
The polymerase chain reaction conditions consisted of incubation for 2 minutes
at 94°C, followed by 30 cycles for 10 seconds at 94°C, 30 seconds
at 60°C, and 2 minutes at 68°C. Polymerase chain reaction products
were separated by agarose gel electrophoresis, purified using silica gel beads
(Roche), and sequenced directly according to a radiolabeled chain terminator
cycle-sequencing protocol (Thermo Sequenase; Amersham Biosciences, Braunschweig,
Germany) by using the gene-specific primers as sequencing primers.
RESULTS
CLINICAL FINDINGS
The main complaint for 13 patients was easily pluckable hair. The number
of haircuts ranged from none from birth to 1 every 2 months. Nine patients
had thin, lusterless, and/or dry hair. Unmanageable hair was noted in 4 patients;
hair was described as being rough, messed up, or hard to comb. It was more
evident in the occipital region in 2 patients. Last, when noted, hair length
was reported as short or variable. It did not exceed 20 cm.
All children were in good health. Eyebrows and eyelashes were normal.
Nails were normal, except for one patient who had fragile nails. One patient
had hypodontia, and lacked incisors and premolars (Table 1).
|
|
|
|
Summary of the Clinical Findings in the 17 Children
|
|
|
A trichogram was obtained in 16 patients according to a routine technique
of sampling hairs in 3 sites (frontal, temporal, and occipital). Examination
by light microscopy revealed a prevalence of dystrophic anagen hairs, and
a low count of telogen hairs for 14 of the 16 patients (Table 1). These dystrophic anagen hairs were devoid of root sheaths,
had a distorted bulb, and had a tapered end (Figure 1). For the 2 other patients, results showed mostly normal
anagen hairs. Nevertheless, dystrophic anagen hairs were still numerous (37.3%
and 19.3%, respectively) and clinical examination and pull test results were
positive for LAHS.
|
|
|
|
Figure 1. A, A typical trichogram showing
almost only dystrophic anagen hairs. B, Detail showing ruffled cuticles and
distorted bulbs.
|
|
|
The family history was positive for LAHS in 5 patients. Three of them
had 1 adult relative (1 mother, 1 father, or 1 paternal aunt) who displayed
clinical signs of LAHS. The 2 other patients with a positive family history
of LAHS (1 brother for one; a father, a brother, and a sister for the other
one, corresponding to family 7 detailed in Figure 2) displayed, among normal or loose anagen hairs, a special
type of curly hairs. These were shorter, hypopigmented, and easy to pluck,
corresponding to the clinical phenotype of diffuse partial woolly hair (DPWH)
(Figure 3).
|
|
|
|
Figure 2. Pedigrees of families 2, 3, and
7 who are affected by loose anagen hair syndrome. DNA samples were obtained
from all individuals. Black symbols indicate clinically affected members of
the families; gray symbols, individuals who are clinically not affected but
carry the K6HF E337K mutation; and open symbols, individuals
who are not clinically affected and who do not carry the mutation. In family
7, diffuse partial woolly hair was diagnosed in I:1, II:1, II:2, and II:3.
|
|
|
|
|
|
|
Figure 3. A patient with partial diffuse
woolly hair. A, Clinical features showing a mixture of curly and straight
hairs. B, Polarizing microscopy: torsion of a hair shaft in a woolly hair.
|
|
|
INDIRECT IMMUNOFLUORESCENCE MICROSCOPY STUDIES
Sections of a scalp biopsy specimen of a patient with LAHS (patient
2) were reacted with specific K6 and K6hf antibodies. Figure 4 shows a near-longitudinal section in which the K6hf antibody
decorated the entire CL. K6 was coexpressed with K6hf in the CL; however,
this occurred only above the widening of the outer root sheath. At this level,
the outer root sheath also started to be positive for K6. The appearance of
the CL is not visibly different from that published previously for hair follicles
of healthy individuals.6
|
|
|
|
Figure 4. Expression studies of K6hf and
K6 in a follicle with loose anagen hair syndrome (LAHS). A near-longitudinal
section of a follicle with LAHS was reacted with an antibody against K6hf
(red) and K6 (green), as described by Winter et al.6
ORSsb indicates outer root sheath, suprabasal; ORSb,
outer root sheath, basal; cl, companion layer; co, cortex; and dp, dermal
papilla.
|
|
|
IDENTIFICATION OF A GLUTAMIC ACID AND LYSINE MUTATION, E337K, IN THE
L2 LINKER REGION OF K6HF
The pedigrees of the 3 families positive for LAHS (families 2, 3, and
7) are shown in Figure 2. Analysis
of the region encoding the helix initiation motif of K6HF did not reveal alterations from the reported sequence in affected
and unaffected members of the 9 families studied. The primer pair used amplifies
not only the helix initiation motif coding region but also considerable parts
coding for the head domain and the -helical 1A subdomain of K6HF. Except for some polymorphisms, these sequences were identical
in all families. The same holds true for the K6HF
helix termination motif coding region contained in the approximately 9000–base
pair polymerase chain reaction product obtained with primer pair 2 (results
not shown). However, successive sequence analysis of the 9000–base pair
segment, which spans from exon 2 to exon 9 of the K6HF
gene, revealed a heterozygous G A point mutation and an adjacent TC
mutation (sequence ladder b in Figure 5)
in affected individual II:1 of family 3. While the TC mutation was silent,
the GA mutation led to an E337K substitution in the K6HF molecule (Figure 5). Whereas both point mutations were
clearly absent in clinically unaffected control individual I:1 of the family
(sequence ladder a in Figure 5),
the same mutation pattern, including the silent TC mutation, could be
detected in clinically unaffected individuals I:2 and II:2 of family 3. The
GA point mutation affects the fourth amino acid position (glutamic acid)
of the short L2 linker region, which spans from S334 to W341 of keratin K6hf
(Figure 5). Investigations in 50
healthy individuals did not reveal the presence of the TC or the GA
mutation in the K6HF gene (results not shown).
The results of subsequent analysis for the K6HF
E337K mutation in the other families were completely negative for members
of families 1, 4 to 6, 8, and 9. In contrast, in family 7, the GA mutation
and the resulting E337K substitution could clearly be detected in clinically
affected individual I:2 and children II:1, II:2, and II:3. None of these individuals
exhibited the silent TC point mutation observed in some members of family
3.
In family 2, the K6HF E337K mutation was clearly
present in affected individual II:2 and in the clinically unaffected father
I:2. As expected, the mutation was absent from the unaffected mother I:1.
It also clearly was lacking in the child II:1. This child was first seen at
the age of 12 months, with alopecia of the occipital area, possibly due to
the pillow. A trichogram was obtained at the age of 3 years and showed many
dystrophic anagen hairs (43%). However, the occipital alopecia had completely
regressed. Other signs of LAHS were totally absent (there was normal growth
with regular cuts, no easy plucking, no sparse hair, no patch of alopecia,
and a negative pull test result). The diagnosis of LAHS was then excluded.
COMMENT
Loose anagen hair syndrome may not be as rare as has been thought. Sinclair
et al,8 in a large series of 43 patients, estimated
the incidence to be 2 to 2.25 cases per million per year. The clinical presentation
of children in our series is similar to that of other cases reported in the
literature.4-5,8-20
The children have slow-growing hair that seldom requires cutting.4-5,8-19,21-22
Parents may also be worried by the patients' diffuse hair loss or localized
patches of alopecia.4-5,8-16,19, 22-23
They may have easily pluckable hair, although this sign is not always obvious.9-10,12-15,19, 21, 23
However, as in our series, the pull test result is usually positive, with
more than 50% of dystrophic anagen hairs per pull in pediatric cases of LAHS.
The presence of loose anagen hairs in children on a gentle hair pull is not
diagnostic of LAHS when 1 to 2 dystrophic anagens per hair pull are found.20 Additional findings include thin, dry, lusterless,4, 9-10,12-14,16, 18-19,21-23
or unmanageable hair,8-9,12-13,17-19
with the occipital area being the most frequently affected region. Sometimes,
hair is also reported as sticky5, 11
or tacky.8
Loose hair anagen syndrome may be an inherited condition. The pattern
of affected family members seems to be that of an autosomal dominant inheritance.5, 8-10,21, 24
In our series, 5 children had 1 or more affected family members. For 3 of
them, relatives displayed clinical characteristics of LAHS. For the 2 others,
family members had hairs of the DPWH type.25-27
The anomaly comprises apparently normal straight hairs and abnormal curly
hairs diffusely intermingled. Some characteristics of LAHS and of DPWH are
quite similar (age at onset, female predominance, hair loss, thin hair, curly
or unmanageable hair, and longitudinal grooves on microscopic examination).
These 2 diseases may, therefore, be somehow related. Furthermore, Sinclair
et al8 recently noted a woolly hair appearance
for 21 of their 24 patients studied.
Based on the pathological features of LAHS, we anticipated that mutations
in hair keratins should not be the cause for the syndrome. Indeed, mutation
analyses of all known hair keratins of both types in the available families
with LAHS did not reveal alterations of the gene structure in affected individuals
(results not shown). In view of the cleavage zone between the IRS and the
hair shaft in the hair follicles of persons with LAHS, we speculated that
mutations in keratins expressed in the IRS might be responsible for the observed
defect. Unfortunately, keratins expressed in the IRS are not yet known. In
contrast, in the apposed CL, connected via desmosomal junctions with the Henle
layer of the IRS, a specific keratin, K6hf, has recently been described.6 Indeed, mutation analysis of the K6HF gene revealed a GA substitution in the region coding for
the L2 linker of the rod domain of K6HF, leading
to a replacement of glutamic acid residue 337 by lysine in 3 of the 9 families
analyzed. Up to now, keratin mutations in linker regions, causative for epidermal
genodermatoses, ie, the Weber-Cockayne syndrome type epidermolysis bullosa,
have only been reported for linker L1/2.28
However, because recent investigations emphasized the importance of the highly
conserved linker L2 for the correct axial alignment of keratin molecules,29 mutations in this non–-helicoidal part
of the K6HF rod domain may also affect intermediate
filament assembly. Because our immunofluorescence studies did not reveal discernible
alterations of the CL in the follicles of those with LAHS, it might be that,
unlike mutations in the helix initiation or termination motif of the rod domain
of keratins, the observed L2 mutation does not lead to a visible breakdown
of the intermediate filament network, but rather to a general destabilization
of the latter.
Based on molecular studies, a dominant inheritance of LAHS was confirmed
in the 3 families in whom the mutation was found, because both children and
fathers bore the mutation. However, father I:2 and child II:2 in family 3
seemed clinically unaffected. In family 7, in which the association of LAHS
and DPWH was found in propositus II:1, the father (I:2) had DPWH and the other
children (II:2 and II:3) had mild LAHS and associated DPWH. This could be
due to a variable penetrance of the condition. Another explanation could be
provided, for the father of family 3 only, by the natural improvement of LAHS.
When comparing phenotypically tested patients according to the presence
or absence of the E337K mutation of K6HF, characteristics
were not different (age at onset, hair growth, positive family history of
LAHS, association with the DPWH phenotype, and trichogram results). Another
gene may, therefore, be implicated in the patients who tested negative for
the mutation. Because the type I partner of K6hf is still unknown, we restricted
our mutation analysis to the K6HF gene. Another explanation
could be provided by the coexistence of major and minor genes. The K6HF gene involved may be one of the minor ones, the major one yet
to be discovered.
Loose anagen hair syndrome is a recently described hair disease, well
defined by its clinical findings and trichogram characteristics. The results
in our series of 17 pediatric patients are similar to other findings in the
literature. Other hair disorders, such as DPWH, may be associated with LAHS,
or even linked in a yet unknown manner. Future case reports may confirm our
findings. Our experience with minoxidil therapy is encouraging, but needs
to be confirmed in a controlled trial. We have, for the first time to our
knowledge, authenticated a keratin mutation, E337K in K6HF, in patients with LAHS, which is possibly causative for this syndrome
in 3 of the 9 families studied. It remains to be seen if another keratin,
and possibly the type I partner of K6hf, is responsible for LAHS in other
patients or if the gene involved is a minor gene, the major one yet to be
discovered.
AUTHOR INFORMATION
Accepted for publication June 18, 2001.
This study was presented at the joint meeting of the Société
Française de Dermatologie Pédiatrique and the British Society
for Paediatric Dermatology, Paris, France, January 11, 2001.
Corresponding author: Alain Taïeb, MD, Service de Dermatologie,
Hôpital St André, 1 rue Jean Burguet, 33075 Bordeaux CEDEX, France
(e-mail: alain.taieb{at}chu-bordeaux.fr).
From Unité de Dermatologie Pédiatrique, Hôpital
Pellegrin-Enfants, Bordeaux, France (Drs Chapalain, Le Roy, Labrèze,
and Taïeb); the German Cancer Research Center, Heidelberg, Germany (Drs
Winter, Langbein, and Schweizer); and the Department of Dermatology, University
Hospital, Belgrade, Yugoslavia (Dr Nikolic). Dr Taïeb is now with the
Service de Dermatologie, Hôpital St André, Bordeaux, France.
REFERENCES
| |
1. Winter H, Rogers MA, Langbein L, et al. Monilethrix: mutations in the hair cortex keratin hHb6 cause the inherited
hair disease monilethrix. Nat Genet. 1997;16:372-374.
FULL TEXT
|
WEB OF SCIENCE
| PUBMED
2. Zaun H. Syndrome of loosely attached hair in childhood. In: Happle R, Grosshans E, eds. Pediatric Dermatology:
Advances in Diagnosis and Treatment. New York, NY: Springer Verlag
NY Inc; 1984:64-65.
3. Nödl F, Zaun H, Zinn KH. Gesteigerte Epilierbarkeit von Anagenhaaren bei Kindern als Folge eines
Reifungsdefects der Follikel mit gestörter Verhafftung von Haarschaft
und Wurzelscheiden. Akt Dermatol. 1986;12:55-57.
4. Hamm H, Traupe H. Loose anagen hair of childhood: the phenomenon of easily pluckable
hair. J Am Acad Dermatol. 1989;20:242-248.
WEB OF SCIENCE
| PUBMED
5. Price VH, Gummer CL. Loose anagen syndrome. J Am Acad Dermatol. 1989;20:249-256.
WEB OF SCIENCE
| PUBMED
6. Winter H, Langbein L, Praetzel S, et al. A novel human type II cytokeratin, K6hf, specifically expressed in
the companion layer of the hair follicle. J Invest Dermatol. 1998;111:955-962.
FULL TEXT
|
WEB OF SCIENCE
| PUBMED
7. Smith FJD, Jonkman MF, Van Goor H, et al. A mutation in the human keratin K6b produces a phenotype of the K17
disorder pachyonychia congenita type 2. Hum Mol Genet. 1998;7:1143-1148.
FREE FULL TEXT
8. Sinclair R, Cargnello J, Chow CW. Loose anagen hair. Exp Dermatol. 1999;8:297-298.
PUBMED
9. Baden HP, Kvedar JC, Magro CM. Loose anagen hair as a cause of hereditary hair loss in children. Arch Dermatol. 1992;128:1349-1353.
FREE FULL TEXT
10. Tosti A, Peluso AM, Misciali C, Venturo N, Patrizi A, Fanti PA. Loose anagen hair. Arch Dermatol. 1997;133:1089-1093.
FREE FULL TEXT
11. Thomas L, Robart S, Balme B, Moulin G. Syndrome des cheveux anagènes caducs. Ann Dermatol Venereol. 1993;120:535-537.
WEB OF SCIENCE
| PUBMED
12. Pride HB, Tunnessen WW Jr. Picture of the month: loose anagen syndrome. Arch Pediatr Adolesc Med. 1995;149:819-820.
FREE FULL TEXT
13. Lalevic-Vasic B, Polic DJ, Milinkovic R. Le syndrome des cheveux anagènes caducs. Ann Dermatol Venereol. 1990;117:701-707.
WEB OF SCIENCE
| PUBMED
14. Grimalt R, Barbareschi M, Menni S, Caputo R. Loose anagen hair of childhood: report of a case and review of the
literature. Eur J Dermatol. 1992;2:570-572.
15. Martinez JA, Velasco M, Vilata JJ, Quecedo E, Aliaga A. Loose anagen syndrome: a new case [letter]. Acta Derm Venereol. 1994;74:473.
WEB OF SCIENCE
| PUBMED
16. Tosti A, Misciali C, Borrello P, Fanti PA, Bardazzi F, Patrizi A. Loose anagen hair in a child with Noonan's syndrome. Dermatologica. 1991;182:247-249.
WEB OF SCIENCE
| PUBMED
17. Haskett M. Loose anagen syndrome. Australas J Dermatol. 1995;36:35-36.
PUBMED
18. Boyer JD, Cobb MW, Sperling LC, Rushin JM. Loose anagen hair syndrome mimicking the uncombable hair syndrome. Cutis. 1996;57:111-112.
WEB OF SCIENCE
| PUBMED
19. O'Donnell BP, Sperling LC, James WD. Loose anagen hair syndrome. Int J Dermatol. 1992;31:107-109.
WEB OF SCIENCE
| PUBMED
20. Olsen EA, Bettencourt MS, Coté NL. The presence of loose anagen hairs obtained by hair pull in the normal
population. J Investig Dermatol Symp Proc. 1999;4:258-260.
WEB OF SCIENCE
| PUBMED
21. Murphy MF, McGinnity FG, Allen GE. New familial association between ocular comoboma and loose anagen syndrome. Clin Genet. 1995;47:214-216.
WEB OF SCIENCE
| PUBMED
22. Camacho FM, Gata I. Hypotrichosis and loose anagen hair in EEC (ectrodactyly, ectodermal
dysplasia, cleft lip palate) syndrome. Eur J Dermatol. 1995;5:300-302.
23. Azon-Masoliver A, Ferrando J. Loose anagen hair in hypohidrotic ectodermal dysplasia. Pediatr Dermatol. 1996;13:29-32.
WEB OF SCIENCE
| PUBMED
24. Chapman DM, Miller RA. An objective measurement of the anchoring strength of anagen hair in
an adult with the loose anagen hair syndrome. J Cutan Pathol. 1996;23:288-292.
FULL TEXT
|
WEB OF SCIENCE
| PUBMED
25. Ormerod AD, Main RA, Ryder ML, Gregory DW. A family with diffuse partial woolly hair. Br J Dermatol. 1987;116:401-405.
FULL TEXT
|
WEB OF SCIENCE
| PUBMED
26. Lalevic-Vasic BM, Nikolic MM, Polic DJ, Radosavljevic B. Diffuse partial woolly hair. Dermatology. 1993;187:243-247.
WEB OF SCIENCE
| PUBMED
27. Guidetti MS, Fanti PA, Piraccini BM, Barbareschi M, Tosti A. Diffuse partial woolly hair. Acta Derm Venereol. 1995;75:141-142.
WEB OF SCIENCE
| PUBMED
28. Fuchs E. The cytoskeleton and disease: genetic disorders of intermediate filaments. Annu Rev Genet. 1996;30:197-231.
FULL TEXT
|
WEB OF SCIENCE
| PUBMED
29. Wang H, Parry DAD, Jones LN, Idler WW, Marekov LN, Steinert PM. In vitro assembly and structure of trichocyte keratin intermediate
filaments: a novel role for stabilization by disulfide bonding. J Cell Biol. 2000;151:1459-1468.
FREE FULL TEXT
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati  Twitter
What's this?
RELATED ARTICLE
Loose Anagen Hair Syndrome and Loose Anagen Hair
Antonella Tosti and Bianca Maria Piraccini
Arch Dermatol. 2002;138(4):521-522.
EXTRACT
| FULL TEXT
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES
Practical Guidelines for Evaluation of Loose Anagen Hair Syndrome
Cantatore-Francis and Orlow
Arch Dermatol 2009;145:1123-1128.
ABSTRACT
| FULL TEXT
Intermediate Filament Proteins and Their Associated Diseases
Omary et al.
NEJM 2004;351:2087-2100.
FULL TEXT
A Small Deletion Hotspot in the Type II Keratin Gene mK6irs1/Krt2-6g on Mouse Chromosome 15, a Candidate for Causing the Wavy Hair of the Caracul (Ca) Mutation
Kikkawa et al.
Genetics 2003;165:721-733.
ABSTRACT
| FULL TEXT
Loose Anagen Hair Syndrome and Loose Anagen Hair
Tosti and Piraccini
Arch Dermatol 2002;138:521-522.
FULL TEXT
|
